‘This evitjon of Understanding Biology for Advanced Level is acomplete and attractive revision of the bestselling {forall students studying AS- and A-Level biology and related courses. mee A ttprovides full coverage of the new Subject Criteria for biology and all major spectfications. It also includes popular option \ topics such as Biotechnology and Human Health and Disease. Other features which students find helpful when studying) __ biology et this fevel have been fully incorporated and include: > Fully accessible text thatis comprehensive, without ‘excessive detall which can cause confusion > Clear diagrams and lots of high quality photographs; linked to an interactive CD-HOM Divisions into manageable sections with summary tables of information to help organise study and revision ‘Notebook’ sections expiaining other topics which you need to know about for biology such as pH and mole calculations . > “The applications of biology. These are a strength throughout the book. » Project suggestions provided for coursework. Lots of up-to-date examination questions for practics °\ Also available to purchase from Nelson Thames IMAGES of BIOLOGY for Advanced Level CD-ROM <> 188N 978 0 7487 6471 6 - f “'02.) This textbook is even further supported by an FA oteractve resource of photographs and video ‘ips. \ Over 50 sequences of light micrographs, scanning electran micrographs, video clips with sound and further explanations are cross-referenced to this book to enhance your understanding of biology. Licensed users ay print or make digital copies ofthe images for private study projects. x ISBN 978-0-7487-3957-8 a WN , Oe ee ; : | hlGlenn and Susan Toolei ‘Tet © Glenn Toole and Susan Toole 1987, 19911995, 1995, Avtvork © Stanley Thornes (Publishes)Ttd. 57700 2.7 (exéepep. 35: 59,998, 400, 480,481, 508, 527 9 Anabel Milne) 380 All rights reserved’ No fott-ofthis'pdbticatigh may Bel 5 j reprodiced or trangihitted in any formn or by alymedns/, «° £ sleczonc or medial lang phtooo) zee or ‘any information storage ad setieval system, without, permission in writing from the publisher or uncer licence rom the Copyright Licensing Agency Limited, Further details of such licences (fr reprographie reproduction) may be obtained from the Copyright Licensing Agency Limited, of Safon House, 6-10 Kirby Stet, London ECIN 81S ‘The right of Glehn and Susan Toole tobe identified as authors of this workhas been asserted by them in accordance with the Copyright, Designs and Patents Act 1983. Originally published in 1987 by Hhitchinson Education, Second edition published in 1981 ‘Thre eiton published in 1995 Fourth edition publised in 1959 by Stanley Thornes (Publishers) Ltd Reprinted by Nelson Thornes Lid Dalin Place 2 Bath Road Cheltenham GLSS 7TH United Kingdom 1213 1415/15 14 ‘A catalogue record of this book is available from the British Library. ISBN 978,0 7487 3957 8 E Fhroughout this book a CD-ROM icon is used to indicate vvhere links exist fo the CD-ROM, The CD-ROM provides ‘ditional support described on the back caver of the book to urther aid your understanding ofthe topic. rtuvork by Oxiord Designers & Illustrators, Peters & Zabransky, lardlines, Tech-Set Lid, Geoff Jones, Annabel Milne, ngela Lumley, Mark Dunn, Tim Smith and David Oliver xpeset by Tech-Set Lid, Gateshead, Tyne & Wear ‘inted and Bound in China by-1010 Printing International Led Acknowledgements i AER Ay To Annabel Milne for permission to reproduce artwork on : 380, 481, 50 "ones di = at ‘Thesis and puss nro ening aml Sind pms to teproa exaniation questions ‘Accord Cini nr London Exmoor cision Northern Geaminatrs and Aan Bord Nother ell Cove Crick amination a Lalvesty of Cambege Lol Examination Syst carpe Lives of ford Deegcy ofc Exomratons) ‘Wolk ent Edoenion Gata ‘The authors and publishers ar grateful othe following for permsion to 8 ‘reproduce phatogrpis and wilecnatera ae falons 5 AEA Tesla: Ares 346 (btm ohn Mason): Biophos Asso (lp) 620 tim) 14 (eh eight photo), Io, 20 Se {tetany}, 218 top 25 atm) 37272 eighth 28,288,270 £51463 foton) i, 50, 310 38,57, 578 617 Bruce Clemons Ce “Toylr 225 Alan Compt 271 top llt-Dr FrldorSsuer 3 (Gon Langs) 36 (Kin Talo), 67 totem fon Norn 37 cae 2741D: Noconan yer) 8 ito Deven Sl (Eat oto: 357 (Ante Holbek Eocene! (p= fank Bocas (Gost Breven) 269 op =DT Growescl) 33 boom Anew DLT Brown) 38 (Nick Fars), 36 oom - Aro Brn) 199 op: Bed Kah i (W Plewon) Enzermarsa Pitre vary 28 ane Frank Lane icure Agency: op“ Plann} 3 op-Lifeseer {$C Allo} 8 (Mark Newrean) 3 (Leonard Use Res) Card Fhotlrarye (Clin Mika} Cane Cow 312 Gop) Ceoechnee te Libary: 278, 346 htt). 2 (2 Haman, Bos eat Angel Boa: 1,24 21,35, 338,359 Hol Static rnena {Gel Nigl Cain 28 op 387 Ug Spence) 32 Nigel Catlin Gop 379 tottam=Niel Cain op Reha Amos 7 8 Spend a Icce 34 (Alin Compost | ant Pafecdaol eal {7 ia Lowe) Martyn China 3, $96 (opr Onna Scented ee (bate London Stic Hl 8 (Geo cg fur pel ‘aid Thompuny 205) Koen 36 ndon Sele Fm) 2S Roy) 290 Dad Petr) 2 fop-Set Cine 305 fata tr Selec Hs) 317 (KG Work, Chop) 953 (raurnes Coll 38 Sree 3 "Wesker 8 Gt - Kah A (CC Gardener) 17 Fran Alen 3 liom + Nowe fusing 05 fk 3M Austen, Animas Annas $35 (Daid Fon Se beige eran) 371 Dovid thompson 385 (Cohn Mire Pass tars = Cows} 07 Gop Hare) 913 an Spree) hls All Publchene 3 Ralston Photograph; Rebere 16,36 op fan Gif ence Mtnary 7 fray Bulb $B ilichard Kit) 31 (Philippe Pin) 36 © Reef Schad, 54 foatom -Chis rel) 3 (Biloy Maan 38 (op Pots ‘Mats srt T Noga) atom Seed /Lssgue Rosca CFD (Croasors PAs and Nase (ye cf Scene 780 tape CN {iphoto Asoc) £0 op Bruen fnxton Eject Saye 124 mon Faser/ RVI Newest upon Tye) La hlipe sly) Ea 128 David Fae), 34 (gh, 36 ex photas-CNKT HE toro Health 163 (Ds fers Burge, 21nd 23 (ap and bottom) 2h (toon) 23 (Profs PA Sti © Matec ons 8 Nes ItttomDr Yorgte Nios top (Befrem Tere Barges 298 (Professor pete Ato: Unnenay Sapna st ne a PCy fr ne CA Rey a an ‘ars Porno Si (arta Bend, 37 ote NONSTE). 373 Ceinor Fraser) 391 (a A These) 02 (B41 Walker) 298(Clnade Nusa s 0 (Prodessovs Mats, Core | Noll, Univeral Laan, Rome) 1 (Allied Pascal 403 top. Asked fad Haneiedee Mich baton Nand Kage) 41 Miopiots Arona 413 420(CNRty 422 Professors He Rautmann nd Dr] RGnock Lae (slain Oohm 232 (PotesorsP Ain and S Cartes) (27 Eamnon ‘MeNiy)438 Biophote Asccute} 48 Candie Syed 459 (rletemy| Borge 54 (Andrew Syed) er (lop~ Amare Syed) 487 (Nar | Kedeai, NUCLA) 511 Peo. Pett Dept of Attn Ui, Ta Sapien ome 530 (De Den Feo, 53 (CNR), si (De Colin Chambiy) 536 Gop Tim Beddos mtdl-Calherne Powe tom), 58 top Sl Longest ‘ote Adan Hr-Davies) 258 (Aste and Hanne rider icler 338 (Cue Naidsarey and Movie Perennoa) 56 (Onogy Md, 367 ech Lecaqu, Rust UCLAF. CNA}, lames King ome) Ci8(A | ost 2 [Ev of Scere), 33 (IP, VENI) Gener Sarge) 6? (CMAN, 6 Chhigoe iow Caerine/CNKIl Science Pictures Liedted 7 5,92 88 26 209), 34,25, 22 (op) 234 24, 71 398 (nam 2b, 3, 3,369, 313d ard boon 7,384 op) 484439 | {on 4 Gp it 48, 512350 Sif Pctures 42 (Thetas Raupach) 6 (Wri Eda) Tory Sto ages (hyp-Newreonl sal Ura Hato Soundanas 213 a Ret caer 9 on care) eB BIC ils, 485 dns Sea) Tapa Petuepoine ae, Asmate | pf Pras Unters ot inser 38209 4 Dileony Ber ft has een nae cata opi es Thepublhors | pings to anor whose radars taen veo ae a app ‘cl any ronor corsa cast porte35 35 37 41 2 43 4a a7 a 51 a ” 7% B 81 8 85 88 7 Chapter 6 Inheritance in‘ context Chapter? DNA and the genetic code 7.1 Evidence that the nucleus contains the hereditary material : 7.2. Bvidence that DNA is the hereditary material 7.3 Nucleic acids 7.4 DNA replication 75 The genatic code 76 Protein synthesis 77 Genetic engineering ' 7.8 Genetic fingerprinting 79 Questions Chapter8 Cell di 81 Chromosomes 82 Mitosis 8.3. Meiosis (reduction division) 84 Comparison of mitosis and meiosis 85 The significance of cell division 8.6 Questions Chapter9 Heredity and genetics 9.1 Mendel and the laws of inheritance 9.2. The test cross 93 Sex determination 94 Linkage 95 Allelic interaction 9.6 Gene interaction 9.7 Questions Chapter 10_ Genetic change and variation 10.1 Methods of recording variation 102 Types of variation 108 The chi-squared test 104 The Fest 105 Origins of variation 106 Causes of mutations 107 Genetic screening and counselling 10.8 Questions Chapter 11 Evolution 111 Population genetics 11.2 Evolution through natural selection (Darwin /Wallace) 105 105 105 109 M3 1s 6 ng. 128 130 134 134 135 139 143 4 148 151 11 158 160 161 168 vw 172 7 7 179 181 184 196 193 193 195a ¢ (CONTENTS 113 Natural selection « .- +202, 114 Artificial selection . 205, 115 Isolation mechanisms : 207 ‘116 Questions 7 210 Chapter 12 Reproduction, development and growth 213 12.1 Comparison of asexual and sexual reproduction 213 422 Asexual reproduction», 215 123 Reproduction in flowering plants: + So gi8 12.4 Fertization and development loweringplans 224 125 Repfodiaction in maminials 126 Sexual cycles En 127 Ferilization and develapment in manmals 287 128 Growth 251 129 Questions 259 Chapter 13. Energy and organisnis 266 131 Firstlaw.of thermodynamics 266 18,2 Second law of thermodynamics, 266 433 Energy and life 267 Chapter 14 Autotrophic nutrition (photosynthesis) 269 1A Leaf structure 269 U2 Mechanism of light absorption 273 143. Mechanism of photosynthesis 25 “Vit Factors affecting photosynthesis 280 145 Questions 285 Chapter 15, Heterotrophic nutrition 290 18.1 Holozoic nutrition 291 152 Diet 291 153 Principles of digestion 295 154 Digestion in humans > 296 155 Adaptations to diet 305 156 Nervous and hormonal control of secretions 306 157 Parasitism _ 308 158 Saprobiontism an 159 Mutualism 312 15,10. Questions aid Chapter 16 Cellular respiration 316 16:1, Adenosine liphosphate (ATP) 316 162 Glycolysis 318 163 Krebs (tricarboxylic acid) cycle 319 6A Electron transport system 321 165 Anaerobic respiration (gnaerobiosis) 325 166 Cotiparison of energy yields 325 167. Alternative respiratory substrates 327 168 Respiratory quotients 329 5169" Questions 330 Chapter 17 -Energy'and the ecosysterii~- 17 Energy flow through the ecosystem 172 The cycling of nutrients * 173 Ecological factors.and their effects on distribution 7A Ecological techniques, 175 Estimating population size: 176 Populations and communities 177 Questions Chapter 18 Human activities and the i ecosystem. 18.1 The impact of pre-industrial humans on the environment, 182 Exploitation of natural resources 183 Pollution 184 Air pollution 185 Water pollution 186 Terrestrial pollution 187 The impact of agriculture on the environment 188 Conservation 189 Questions Chapter 19 Why organisms need transport and exchange mechanisms Chapter 20 Gaseous exchange 20:1 Respiratory surfaces 20.2. Mechanismsof gaseous exchange 20.3 Control of ventilation in humans 20.4 Measurements-of lung capacity 205 Effects of exercise onbreathing and gaseous exchange 206 Questions Chapter 21 Blood and circulation (ansport in animals) 21.1 Structure of blood 21.2 Functions of blood 213 The immune system 21.4 The circulatory system 21.5 Heast structuze and action 21.6 Lymphatic system e 2LY Questions Chapter22 Uptake and transport in plants 22.1 The importance of water to living organisms 22.2 Simple plant tissues 223 Water relations of a plant cell 22.4 Transpiration 2255 Factors affecting transpiration 226 Uptake of water by roots, 2.7 Uptake and translocation of minerals 22.8 Translocation of organic molecules 29 Questions 333 334 339 343 354 362 392 395 395 07 407 410 a1 412 413. 421 29 433 440 442. 445; 435 “a7 49 451 4538 462 465 467 anChapter 23. .Osmoregulation and.excretion .476 23a Introduction 232 Exoretory products 23:3 Osmoregulation and excretion in- animals 23.4 The mammalian kidney 235 Hormonal control of osmoregulation and ‘excretion 23.6 Questions Chapter 24 How control systems developed Chapter 25 Homeostasis \ 25.1 Principles of hoxhcostasis 25.2 Temperature control 253 Control of blood sugar 25.4 Control of respiratory gases 25.5 Control of blood pressure 25.6 The liver 25:7 Questions Chapter 26 -The endocrine system 26, Principles of endocrine control 26.2 The pituitary gland 263 ‘The hypothalamus 264 The thyroid gland 265 The adrenal glands 2666 The pancreas 267 Questions Chapter 27 The nervous system 27:1 Nervous tissue and the nerve impulse 272, The synapse 273 The reflex are 27.4 The autonamic nervous system 275 The central nervous system 276 Sensory perception 2727 Behaviour 278 Questions Chapter 28 Muscular movement and support 28.1 Structure of skeletal muscle 282 Muscular contraction 283 Skeleton and locomotion 28.4 Questions 76 976 a7 79 88 526 526 534 538 540 541 57 555 561 565 565 567 Ss” 575 Chapter 29 Control systems in plants 291 Plant responses 29.2 Plant hormones 29.3 Control of flowering 294 Questions Chapter 30 Biotechnology 30.1 Microorganisms 302 Growth of microorganisms 303 Industrial fermenters and fermentation 304 Biotechnology and food production 305 Biotechnology and pharmaceuticals 306 Biotechnology and fuel production 307 Biotechnology and waste disposal 308 Biotechnology and agriculture 309. Other producto the biotechnology dustry 30.10 Cell, tissue and organ culture 301 Questions Chapter 31 Human health and disease 311 Principles of human health 312 Infectious diseases 313. Inherited diseases 314 Degerferative diseases 315 Mental illness 31.6 , Human inflicted diseases 317 Deficiency diseases 31.8 Protection from disease 31.9 Detection of disease 31.10 Questions Chapter32_ Food, diet and health 32.1 Balanced diet : 32.2 Malnutrition 323 Food preservation 324 Food additives 325 Questions Further Questions Appeuitiv: The water molecule Glossary Index 594 594 595 610 on oi 618 615 616 623 626 626 628 638 638 640 640) a2 682 67 650 688 661 666 670 on. 681 683 689id Tevel Biology. specifications (previously called labisies)valong with the’ Awarding Bodies that produce say, have changed. over the past few years. One major ‘Ghange has been. the introduction of Advanced Subsidiary “{ASGlovel) and A2 specifications sw Advanced Subsidiary specifications are examined at a Slandard expected.of candidates who have completed the “fiBt halfeof-a full Advanced Level course. AS such, it _Xgécupies place intermediate between GCSE and Advanced ‘fevel. Tt can either be a qualification in its own right or a " Mepping-store towards a full Advanced Level. An AS-Level ‘dan be obtained after one year of study with a further year {celled A2) being required to convert it to the full A-level. " All biology spécfications include a core of tapics (called the _ Subject Criteria) which is common to all and which builds ‘upon the knowledge and understanding of Science in the National Curriculum, All specifications are divided into ‘units (modules) which can either be taken at intervals ‘luring the course or stacked together at the end. A practical investigation or project is also a common feature. Detailed analysis ofall the AS-level and A2 specifications has ensured that’ this latest edition of Understanding Biology for ‘Advanced Level gives a clear and comprehensive coverage of these topics and many others which may bé optional in your AS-level or A2 specifications. ‘The book is primarily intended for students taking AS-lével ‘and -A-level (A2) biology, but will also be valuable to students’ studying’ the Scottish Higher Grade examination, ‘Advanced “GNVQ. Science -and ~the ~ International Baccalaureate. Style and accessibility have always been a strong feature of this book and its numerous diagrams have been further ~-énkanced by the iitroduction of many thtee-dimensional drawings which, improve understanding, Likewise. the frequently used tables have been supplemented by detailed charis whicl-summarize the essential points of a particular topic. Many more photographs have been introduced to add inlefest, ai understanding end to add reality to the subject. The ‘Notebooks’; giving short explanatory sections on key topics which underpin biology, have been retained whilé he applications have been expanded in number and renamed ‘Biology around us’ to reflect their broader coverage of relevant materials To pride ita for indGpenden,practial work, “Prje sipgestons’ are also retuned antes hopes Dat nut’ continue to provide bose semarkate hale open of iniommation which not only. put things into perspective but ace provide nvereatngandwodinhilemetetee Three major adelitions are, firstly, inclusion ofa new chapter on Human Health and Disease which covers in detail this Popular option in AS-level and A2 specifications. Although ‘material on human health has been brought together in a igle coherent unit to assist study ofthis topic, information {s still integrated into the rest of the book either in its own Fight or by cross-eferencing tothe new chapter. Secondly a ew chapter on Food, diet and health has been added to meet the requirements ofthis increasingly common option, Finally, a ‘Glossary’ has been included to enable the reader te quickly research the definition of al the most commonly used biological terms in the book ‘The transition from GCSE to AS-level is not an easy one and the book has been written in a manner which makes this process smoother. To further assist this change the authors have produced a Course Study Guide, which complements this core textbook. In addition to providing help on fractcal Work and answering examination questions, i also includes ‘most of the diagrams-within the book which can then be annotated and labelled as you wish and included in your own nates A further exciting addition to this range of publications is Images of Biology for Advanced Level CD-ROM. Packed with light and scanning electron micrographs, as well as video clips, it isan interactive resource which runs on a PC. Written text; as well as a sound commentary, provide @ wealth of emphasized key points and information, The user is able to tour around a specimen or magnify parts oF it as they choose as if-they had their own microscope. The resource brings biology to life in a way no textbook ever could. All these linked resources and this core textbook in Particular ate intended to provide clear, highly readable and easily undersioed information to the average student, 7 textbook contains fufficient detail t0 satisfy the requirements of all the major specifications without the sometimes unnecessary detail ‘which can cloud the underlying issues, We trust that this book will contribute fo examination Success while engendering a genuine lave of biology which ‘will stimulate the reader to delve further and deeper into the subject. We would like to express our gratitude to Wilbert Garvin for. compiling the project suggestions and to Adrian Wheaton, Simon Read, Malcolm Tonalin and all other at Stanley Thornes whose hard work and encouragement have made this fourth edition possible Glenn and Susan Toole lilt section through kidney tubules to show cellular organization (pps)Biology covers a wide field of information over a considerable size range. On the one hand it involves the mbvements of electrons in photosynthesis and on the other the migrations of individuals around the earth. Within this range itis possible to recognize seven levels of organization, each of which foims the basis of the next. The most fundamental unit is the atom; atoms group to form molecules, which in turn may be organized into cells, Cells are grouped into tissues which collectively form. ‘organs, which form organisms. A group of organisms of a single species may form a population. “1/000 000000 (0°) mei a (106) metre Atoms are the smallest unit of a chemical element that can exist independently. They comprise a nucleus which contains ‘positively charged particles called protons, the number of which is referred to as the atomic ttumber. For each proton there is a particle of equal negative charge called an electron, so the atom, has no overall charge. The electrons are not within the nucleus, but orbit in fixed quantum shells around it (see Fig. 1.1). There is, a fixed limit to the number of electrons in any one shell. There may be up to seven such shells each with its own energy level; electrons in the shells nearest the nucleus have the least energy. ‘The addition of energy, eg. in the form of heat or light, may promote an electron to a higher energy level within a shell. Such an electron almost immediately returns to its original level, releasing its newly absorbed energy as it does so. This electron thovernent is important biologically in processes such as photosynthesis (Chapter 14).SIZE AND COMPLEXITY Y eed ‘nemie ivoRosen Peton (oegaivly chix InaSeinersioral ‘ori aound ti uu cARBON ‘ome sumer mera prone Numtoref neuter Relate stomicess, Number est quantum ea ‘Seed euantam cat 7 Fig. 1 Atomic structure of four commonty occurring biological elements tei a =i ae @)._. 8a enue Daapraton one let and ons en. Re eee! propane fe a sae a fe ryategen ao Suthers tbe mas uber “tum atom (Grapeten, en leton and tao ‘nsdrons Age chemi properties fe a sane athe yezogan ao ut has vee nas tha ass number meee wt eaacoe a Lae @ =SeeEaee semen ons, pact Fig. 1.2 Atomic structure of the atoms of Iydrogen, deuteriva, tritium: and helinnt ‘The nucleud.of the atom also contains particles called neutrons which have no charge. Protons and neutrons contribute to the mass of an atom, but electrons have such a comparatively small mass that their contribution is negligible. ‘However, the number of electrons determines the chemical properties of an atom. (See Fig. 1.2.) 11.1 Ions ‘As we haveseen, atoms do not have any overall charge because the number of protons is always the same as the number of electrons and both have equal, but opposite, charges. [fan atom loses or gains electrons it becomes an ion. The addition of electrons produces a negative ion while the loss of electrons gives rise to a positive ion. The loss of an electron is called oxidation, while the gain of an electron is called reduction. The atom losing an electron is said to be oxidized, while that gaining an electron is said to be reduced. The loss of an electron from a hydrogen atom, for instance, would leave a hydrogen ion, comprising just a single proton. Having an overall positive charge it is written as H". ‘Where an atom, e'g, calcium, loses two electrons its overall charge is more positive and itis written Ca. The process is similar where atoms gain electrons, except that the overall charge is, negative, eg. Cl”. fons may comprise more than one type of atom, e.g. the sulphate ion is formed from one sulphur and four oxygen atoms, with the addition of two electrons, SO, 1.1.2 Isotopes ‘The properties of an element are determined by the number of protons and hence electrons it possesses, If protons (positively charged) are added to an element, then an equivalent number of& nineaingraph af nhl lave © electrons (negatively charged) must be added to maintain an overall neutral charge. The properties of the element would then change ~ indeed it now’ becomes a new element. For example, it can be seen from Fig, 1.1 that the addition of one proton, one electron and one neutron to the carbon atom, trasforms it into a nitrogen atom. If, however, a neutron (not charged) is added, there is no need for an additional electron and do its properties remain the same. As neutrons have mass, the element is heavier. Elements which have the same chemical properties as the normal element but have a different mass are called isotopes. Hydrogen normally comprises one proton and one electron and consequently has an atomic mass of one. The addition of a neutron, doubles the atomic mass to two, without altering the element’s chemical properties. This isotope is celled deuterium. Similarly, the addition of a further neutron forms the isotope tritium, which has ani atomic mass of three (Fig. 1.2) Isotopes can be traced by various means, even when incorporated in living matter. This makes them exceedingly useful in tracing the route of certain elements in a variety of biological processes. |sotopes are varieties of atom which differ in their mass, They are usually taken up and used in biological systems in the same way as the ‘normal’ form of the element, but they can be detected because they have different properties. isotopes have been used to study photosynthesis, respiration, DNA replication and protein eynthosis. Isotopes such as °C and °C are not radioactive and so do not decay but they can be detected using a mass spectrometer or a ‘nuclear magnetic resonance (NMR) spectrometer. To use a mass spectrometer the sample to be studied is ‘vaporized is such a wey that the molecules become charged. They then pass through a magnetic field which deflects them and the machine records the abundance of each ion with a particular charge : mass ratio. Isotopes with an uneven number of protons or ‘lectrons spin, like spinning bar magnets. A NMR spectrometer detects each typi of spinning nucleus. Radioactive isotopes can be used in'a different way to follow biological processes. For example, when studying photosynthesis ‘eaves may be exposed to “CO, instead of !°C0,. The ‘labelled’ carboiris incorporated into the carbohydrate produced and can be detecied using autoradiography. This technique relies on the ability of radioisotopes to og’ photographic flm as they emit radiation, whan the < wil cinumelography (see Section 14.3) itis possible to-identify which individual compounds have taken up the radioactive carbon. if an acourate measure of the radioactivity in Sample ls required, a scintillation counter can be used.1.2. Molecular organization eae We have seen that the electron shells around an atom may each 6 Besten contain a maximum number of electrons. The shell nearest the nucleus may possess a maximum of two electroris and the next Hyerogen tom shell a maximum of eight. An atonvis most stable, ie. least Gulcwgernesccrsstel reactive, when its outer electron shell contains the maximum. i Ison antiesemistectee possible number of electrons. For example, helium, with a full complement of two electrons in its outer shell, is inert. In a | eros on = H° hydrogen atom, the electron shell has a single electron and so the | ® Orpcioney.evhoswowet —aiom is unstable. If two hydrogen atoms share their electrons (Fig. 1.3), they form a hydrogen molecule, which is more stable. fyogenmokcie-Hs The two atoms are effectively combined and the molecule is Taal hare. The les rom written as H,. The sharing of electrons in order to produce stable ‘ © © molecules is called covalent bonding. ‘The oxygen atom contains eight protons and eight neutrons in the nucleus with eight orbiting electrons. The inner quantum shell contains its maximum of two electrons, leaving six electrons in the second shell (Fig: 1.1). As this second shell may contain up to eight electrons, it requires two electrons to complete the shell and become stable. It may therefore combine with two hydrogen atoms by sharing electrons to form a water | molecule (Fig. 1.4). In this way the outer shells of the oxygen atom and bath hydrogen atoms are completed and a relatively stable molecule is formed. Carbon with its six electrons (Fig. 1.1) has an inner shell 1 containing two, leaving four in the outer shell. It requires four ‘Tolle thea relavahy sia Fig. 1.3 Atomic structure ofa hydrogen atom, a Iyddrogen ion and ¢ hydrogen moleculebara elect (CH) # “hatin lo hr acne wry aon neh hyrogen ar hus coro ls ua tection nite bon alam comptes alr she with ii aside T08,) ‘Thorton serve locion ith sch onybor lor. A they compas tht a Fig, 14 Atomic models of the molecules of woater,-methaate and carbon dioxide more electroiss to fill this shell. It may therefore combine with four hydrogen atoms each of which shares its single electron. ‘Thig molecule is called methane CH, (Fig, 1.4). It may. also combine with two oxygen atoms, each of which shares two electrons. This niolecule is carbon dioxide (Fig, 1.4) ‘When an atom, e.g. hydrogen, requires one electron to complete its outer shell itis said to have a combining power (valency) of one. Oxygen, which requires two electrons to coinplete its outer shell, has a combining power of two. Likevise nitrogen has a combining power of three and carbon of four. When two atoms share a single electron, the bond is referred to as a single bond and is written with a single line, eg, the hydrogen molecule is HH and water may be represented as H—O—H. If two atoms share two electrons a double bond is formed, It is represented by a double line, eg carbon dioxide may be written as O=C=O. To form stable molecules, hydrogen must therefore have a single bond; oxygen two bonds (either two singles or one double); nitrogen must have three bonds (either three singles, or one single and one double); and carbon must have four bonds. It should now be apparent that these four atoms can combine in a number of different ways to form a variety of molecules. This partly explains the abundance of these elements in living organisms although some are relatively rare in the earth’s crust (Table 1.2), Carbon in particular ean be seen to be almost 200 times more abundant in living organisms than in the earth's crust. Why should this be so? In the first place, carbon with its combining power of four can form molecules with a wide variety of other elements such as hydrogen, oxygen, nitrogen; sulphur, phosphorus and chlorine. This versatility allows great diversity in living organisms. More importantly, carbon can form long chains linked by single, double and triple bonds. These chains may be thousands of carbon atoms jong. Suck large molécules ate essential to living organisms, not least as structural components. Furthermore, these'chains have great stability — another essential feature. Carbon compounds may also form rings. These rings and chains may be combined with each other to give giant molecules of almost infiniie variety. Examples of the size, diversity and complexity. of carbon molecules can be found among the three major groups of biological compounds: carbohydrates, fats and proteins. ‘These are discussed in more detail in Chapter 2 1.2.1 Ionic bonding In addition to foiming covalent bonds through the sharing of ‘elettrons, atoms riy stabilize themselves by losing or gaining eleétrons to form ions. The loss of an electron (oxidation) leaves the:atom positively charged (oxidized). The gain of an electron * (cedhuiction) leaves the atom negatively charged (reduced). Oppositely charged aivins aiitavi one another forming one ‘bonds: Sodium, for example, tends to lose an electron forming a Na* ion; chlorine tends to gain an electron forming a CI~ ion ‘These two oppositely charged ions form ionic bonds and form »* eodiunvchloride (common salt),a ii | sux aN combexry CC ——— i contre 1.2.2.Hydrogen bonds The electrons ih'a molecule do not distribute themselves evenly i , but tend t6 group at one position. This region will consequently i bbe more negative then the rest of the molecule. The molecule is said to be polarized, The negative region of such a molecule will be attracted to the positive region of a similarly polarized ‘molecule. A weak electrostatic bond between the two is- formed. In biological sjstems this type of bond is frequently a hydrogen bond. These bonds are weak individually, but collectively form important forces which alter the physical properties of molecules. Water forms hydrogen bonds, which significantly affect its properties and hence its biological importance. j else 13. Cellular organization _ , In 1665, Robert Hooke, using a compound microscope, discovered that cork was composed of numerous small units. He called these units cells. In the years that followed, Hooke and other researchers discovered that many other types of material were similarly composed of cells. By 1838, the amount of plant ‘material shown to be composed of cells convinced Matthias Schleiden, a German botanist, that all plants were made up of cells, The following year, Theodor Schwann reached the same conclusion about the organization of animals. Their joint findings became known as the cell theory. It was of cénsiderable biological significance as it suggested a common denominator for all living matter and so unified the nature of organisms. The theory makes the cell the fundamental unit of structure and function in living organisms. Hooke had originally thought the cell to be hollow, and that the wall represented the living portion. It soon became clear that cells were far from hollow. With the development of better light microscopes, first the nucleus and then organelles such as the chloroplasts became visible. One hundred years after Schleiden and Schwann put Root cll of maize plant (TEM) (>3000 approx) forward the cell theory, the development of the electron microscope revolutionized our understanding of cell structure. With its ability to magnify up to 500 times more than the light microscope, the electron microscope revealed the fine structure of cells including many-new organelles. This detail is called the ultrastructure of the cell. The complexity of cellular structure so revealed led to the emergence of a new field of biology, cytology ~ the study of cell ultrastructure. This shows that while organisms are very diverse in their structures and cells vary considerably in size and shape, there is nevertheless a remarkable similarity in their basic structure and organization, | ‘This structure and organization is studied in Chapter 4.Portuguese manvof-war (Mysatia eating fish Kidney epitheli (TS) 6 350) ‘The first colonies may have arisen when individual unicells {failed to separate after cell division. Within colonies each cell is capable of carrying out all the essential life processes. Indeed, if separated from the colony, any cell is capable of surviving independently. The only advantage of a colonial grouping is that, the size of the unit probably deters some predators and thus increases the group's survival prospects, Ifpne cell in a colony should lose the ability to carry out @ vital process, it could only survive by relying on other cells in the colony to perform the process on its behalf. The loss of one function, however, might permit the cell to perform one or other of its functions more efficiently, because the energy and resources required by the missing function could be directed towards the remaining ones. In this way, the individual cells within a colony could have become different from one another in both structure and finction, a process known as differentiation. Further changes of this type would finally result in cells performing @ single function. This is known es specialization. Clearly specialization misst be organized in such a way that all essential functions are still performed by the colony as a whole. With increasing specialization, and the consequent loss of more and more functions, any cell becomes increasingly dependent on others in the colony for its survival. This interdependence of cells must be highly organized. Groups of cells must be coordinated so that the colony carries out its activities efficiently. Such coordination between the different cells is called Integration. Once the cells become so dependent on each other that they are no longer capable of surviving independently, then the structure is no longer a colony but a multicellular organism, Attissue is a group of similar cells, along with any intercellular + substance, which performs a particular function. Some cells, e.g. unicellular protozoans and algae, perform all functions which are essential to Life. It is impossible for such cells to be efficient at all funetions, because each function requires a different type of cellular organization. Whereas one function might require the cell to be long and thin, another might require it to be spherical. One function might require many mitochondria, another, very few. Acid conditions might suit one activity but not another. No ‘one cell can. possibly provide the optimum conditions for all activities. For this reason, cells are specialized to perform one, or at most a.few, functions. To increase efficiency, cells performing the same functions are grouped together into a tissue. The study of tissues is called histology. Some organisms, eg. cnidarians, are at the tissue level of organization. Their physiological activities are performed by tissues rather than organs. Examples of animal tissues include squamous and ciliated epithelium (Section 20.2.5). Examples of plant tissues include xylem (Section 22.43) and phloem (Section 22.8.2), :Hloney bee queen surrounded by workers ‘An organ is a structural and functional unit ofa plant or an It comprises a number of tissues whieh are coordinated to, perform a variety of functions, although éne major function’ offen predominates. The majority of plants and animals are composed of organs, Examples include the leaf of plants; and the ale) liver in mammals. Most organs'do not finclion ifidependi but in groups called organ systems: A typical organ systent’ the digestive system which comprises organs Such as the. stomach, duodenum, ileum, liver and pancreas, Certain organs ‘may belong to more than one system. The pancreas, for example, forms part of the endocrine (hormone) System as well as the digestive system, because it produces the hormones insulin and ‘glucdgon, as well as the digestive enzymes amylase and trypsinogen. . A population is a number of individuals of the same species which occupy a particular area at the same time. In itself, a population is not a level of organization as no organization exists between the individual members. In some species, however, the individuals do exhibit some organization in which they cooperate for their mutual benefit. Such a population is more accurately termed a society. It differs from a colony (although the term is often used) in that the individuals are not physically connected to one another, but totally separate. As with a colony, the individuals can survive independently of others in the society, although usually somewhat less successfully. Unlike most colonies, there is considerable coordination between the society members and communication forms an integral part of their organization. Societies may exist simply because there is safety in numbers, e.g. schools of fish. They may enable more successful hunting, as in wolves, or aid the successful rearing of young, as in baboons. In insects, however, the degree of organization is considerable. Thete is division of labour which leads to differentiation of individials in order fo perform specialized functions. In a bee society for instance, the queen is the only fertile female and has purely reproductive role. The. drones (males) also function reproductively while the workers (sterile females) perform a variety of tasks such as collecting food, feeding the larvae and guarding afd clearing the hive. ‘Complex societies can readily be compared to an organism with its organs each specialized for a major function. Some accouint of the organization of a bee colony is given in Section 27.7.5.“apie 21 Inorgatie fons afi theltfusttions in plaiis'and annals ‘Water is the most important inorganic molecule in biology (see appendix i, page 681 for more detail on the water molecule). Dissolved in the water within living organisms are a large umber of inorganic ions. Typically they constitute about 1% of an organism by weight, but they are nonetheless essential. They are divided into two groups: the macronutrients or major, elements which are needed in very small quantities, and the micronutients or trace elements which are needed in minute amounts (a few parts per million). Although the elements mostly fall into the same category for plants and animals, there are a few exceptions. Chlorine, for example, is a major element in animals but a trace element in plants. In addition to the essential elements listed ih Table 2.1, some organisms also have specific requirements such as vanadium, chromium and silicon. ‘Detiden Silewielar pula ahaa ally of tot a the formation of dal, i ainalsleliceicy Gan result ina si : Ive chatns of oie proteis ving ary sricie. A daily in plants causes horsis ot development hie ese onto and al “renin: Adit active tanehoit | Batassium plays an i svn fol ibe wandelcelon ot sean sieteot MOLECULAR ORGANIZATION iat on a8z410N, Tame21 eo. Funions [Need = =e ‘netion, Coes Ta plant calcium pectateis aaj componeniof fhe. {A plane, deny cams en fgg pt : ‘hile lacie of ell alle ep is Lereforesicesnty for a hence stunted growth. ivahimals defen leads the proper ceelpmeng (ae adhe Vestn of | orcas and dey che ction oe eyo : cast of ones teelcand sels Needed for : orig of Hobe and te eb action of muscle ey Helps manvain Wie dace, oprpoisand ‘mania his necessary fr the functioning oF the asion/eation balance across cell membyanes-Asvals | Kidney, nerves and muscles, deficiency may cause fscive ansport of certla materials sca cll ‘muscular eps Sodium i 50 comin in soils (hat | Rembiane A onset rthera acle Jn pens ane | decency npane rae Sohn onshave muh te hele matin giciy fare uncon at pts and may be acanged forthe ‘sip a alla he eereal en and wion falc In animals, deficiency may couse muscular cxampa. ls -| balance across cell nersBraes. Needed forthe formation | widespread avalon soils makes deficiency in #2 | Gehyatoehore satin pas juice Assit i the plans practically unkown _| taneport.of carbon dioxide by blood (cloide sil) “Magiesiusi | A constituent of chlorophyll. An acivaiot for some ‘Deicegyin plants lead io ehlorais Ms" trayines eg ATPase. A componentof bone ad tel roa Fe ‘Acoialtueitof election eacers eg cylodwones, Deficiency in plants leads to chlorosis and in animals fo ore ‘reeded'in vespration and photosynthesis A constituent | anaemia ‘of certain enzymes, .g dehydrogenases decarboxglass, ‘peroxidases and catalase. Required in the synthesis of ' SloropiylForns part ofthe haem group in respisatony pigments such as haemoglobin haemoerthri, myoglobin and dloroessor ‘Micronutrients! trace glements Mangancie || Anactivator of ertatn enzymes, eg. phosphatases, A _ | Deficlency In plans produces leaves mated with grey Me srowth factor in bone devetopnent ain ih animals, bone deformations Copper Cut | A constiuentafsome enzymes, eg eylocome oxidase | Deicene in plants causes young shoots odie back at and tyrosinase, A component ofthe reepicatory pigment | an erly stage haemacyanin : Tedine = ‘Aconslsuent ofthe bosinonethyronn, which congols | Todine snot requied by higher plants. Defiieney ‘metabolism in animals humans causes ratinism in children ane goite in dull in some olher vertebrates it is essential for smelamorphie changes Cobalt CoP: | Constituent of vila By whichis imporiantin he | Defieney in animals causes pernidous ansema sythess BERNA aucleoprtein and eed blo ells Zine Za “Anactvatr of teraln enzymes, eg caonic anhydrase. | Carboni anhydrase imporant ifthe transport of Required in plans forleaf formation thesyntesis of | carbon dionide in vertebrate blood. Deficiency in plans indole acetic acid auxin) and anserbicrespication | produces malformed, and sometimes matiled, leaves (Gleshalie fermertation) : Maysdeua | Requieiy pint or he educon ofnivatew nie | Deficeney podueda eatonn wep ei Nowa Mo nthe formation of amino acs. Esentialforrtzogen | in most animals or Mo" fiation by prokaryotes Boron BO? | Required forthe uptake of Ce by roots Ads the Boron snot required by animal, Decency in plants or BOF germination of pollen grairs and mtolicdivsion in| eauses death of young shoo and abnorinal growth ‘erst May cause specific seas sucha ‘nternal coi of apples and ‘heart ro’ ef beet and celery Fluorine F ~ | A eomponentot teeth and bones Not rire by most plants. Asfoioes with calla 8 fon aun Muoede Which stregthens teeth and help prevent decacad -hloasis (iste) ~ ith healthy plants shown for comparison Carbohydrates comprise a large group of organic compounds which contain carbon, hydrogen and oxygen and which are + either aldehydes or ketones. The word carbohydrate suggests that these organic compounds are hydrates of carbon. Their general formula is C,(H,0),. The word carbohydrate is convenient rather than exact, hecause while most examples do conform to the formula, e.g. glucose (C,H,,0,) and sucrose (Cigtly,O,,) a few do not, eg. deoxyribose (CH,<0,)- } Carbohydrates are divided into three groups: the monosaccharides (‘single-sugars’), the disaccharides (‘double- sugars’) and the polysaccharides ('many-sugars’). This arrangement is typical of many organic molecules where single tunits, called monomers, are combined to form larger units, called polymers. ‘The functions of carbohydrates, although variable, are in the ‘main concerned with storage and liberation of energy. A few, such as cellulose, have structural roles. A full list of individual carbohydrates and their functions is given in Table 2.3 on p. 19. 2 Bc stale acl ‘Monosaccharides are a group of sweet, soluble crystalline niolecules of relatively low molecular mass. They are naried with the suffix -ose. Monosaccharides contain either an aldehyde group (—CHO), in which case they are called aldoses or aldo- sugars, ar they contain a ketone group (C=O), in which case they are termed ketoses or keto-sugars. The general formula for ‘a monosacchaiide'is'(CH,O),. Where n=3, the sugar is called a triose sugar, | a pentose sugar, and n=6, a hexose sugar. ‘Table 2.2 classifies some of the more important monosaccharides.MOLECULAR ORGANIZAHION ‘TARCE 2.2 _ Classification of monosaccharides 2,3:1 Structure of monosaccharides i Probably the best known monosaccharide, glucose, has the formnula C,H;,0,, All but one of the six'carbon atoms possesses an hydroxyl group (—OH). The remaining carbon atom forms part of the aldehyde group. Glucose may be represented by a strdight chain of six carbon atoms, These are numbered beginning at the carbon of the aldehyde group. Glucose in common with other hexoses and pentoses easily forms stable ring structures. At any one timic most molecules exist as rings | rather than a chain. In the case of glucose, carbon atom number 1 may combine with the oxygen atom on carbon 5. This forms a six-sided structure known as a pyranose ring. In the case of fructose, itis carbon ator number? which links with the oxygen on carbon atom 5. This forms a five-sided structure called a | furanose ring (Fig. 2.1). Both glucose and fructose can exist in both pyranose and furanose forms. Straight chain arrangements , sgHO grow iop—on i } (PHOH . euycose Faucrose Ring arangemens gow s—4 GHOH -O. (HOH a Vl ’ 8 i si i U7 iN, of Nps — . H a H OH GLUCOSE peatucose FRUCTOSE PYRANOSE Nas FURANOSE FING Fig. 2:1 Strucee of ovens isomers of gluse nu fructoe tansoainnan cern nee ia eat aantl Glucose, in-common with most carbohydrates, can exist as a number of isomers (they possess the same molecular formula but differ in the arrangement of their atoms). One type of isomerism, called stereoisomerism, occurs when the same atoms, or groups, are joined together but differ in their arrangement in space. One form of stereoisomerism, called optical isomerism, results in isomers which can rotate the plane of polarized light (light which is vibrating in one plane only). ‘The isomer which rotates the plane of polarized light to the tight is called the +-form; the isomer rotating it to the left is called the —form. ‘The mole is the scientific unit for the amount of a substance and is expressed as the symbol mol. 1 mol of any substance contains the ‘same number of particles (atoms, molecules or fons), This number is known as Avogadro's constant and is equal to 6.023 x 10%. To give you some idea of the vast size of this number, itis equal to the total human population of one hundred milion milion worlds, identical to ours! : Different atoms (and therefore molecules and ions) have different masses. Chemists use the atomic mass of carbon, set at 12, as a standard against which to compare the mass of other atoms. Thus hydrogen, which has a mass one-twelfth that of carbon, is given the ‘mass of 1. These are known as relative atomic masses. The relative ‘atomic mass of an element in grams always contains 1 mol ofits atoms {j,6. 6.023 x 10% atoms), The same is true of the relative molecular mass of a molecule. Thus: ‘a mole of hydrogen atoms (H) has a mass of 19 a mole of hydrogen molecules (H,) has a mass of 2g ‘a mole of oxygen atoms (0) has a mass of 16g a mole of oxygen molecules (O,) has a mass of 32g ‘a mole of water molecules (H,0) has a mass of 189. To find out the number of moles in a given mass of a substance we simply divide the mass (in grams) by the mass of 1 mol, e.g. in 90g of water there are #8 mol =5 mol (or 5 x 6.028 x 10° molecules) ‘When dealing with gases, we use volume rather than mass to measure amounts. A mole of any gas at standard temperature and pressure (0°C and 1 atmosphere) occupies 22.4dm: (itres). At room temperature (20°C) this volume expands to 24 dm®. That all gases, regardiess of the mass of the molecules they comprise, should occupy the same volume may seem surprising. in a gas, however, the molecules are so far apart that the size of the molecule itself is unimportant in terms of the volume occupied. Imagine several balls ‘bouncing around inside a large hall - they could all be fitted in whether they were golf bails, tennis balls or footballs. ‘The concentration of a solution can be expressed in moles. A 1 mol dm” solution (1M solution) contains 1 mol in each dm? of thei i MOLECULAR ORG ANZA Different isomers ai MOLECULAR ORG ANIZABION when a carbon atom has four different: groups attached to it. This is called an asymmetric carbon atom. ‘An asymmetric carbon atom arises when glucose forms a ring structure. This gives rise to two isomers, the a-form and the B-form. Both types occur naturally and, as we shall see later, result in considerable biological differences when they form polymers. Fig, 2.1 illustrates both types. solution, In other words to make up a 1 mol dm-* (1 M) solution of a substance we add the relative molecular mass in grams of that substance to 1 dm® (litre) of water, In the case of sucrose (Cigte,0,,) this is: Numberin Relative atomic Molecule. sucrose mass (9) 2 yaxie=t40 HYOROGEN 2 4 22x 122. OXYGEN - rf 16 1118 =178 Total 9429 Hence we dissolve 342g of sucrose in 1 dm® of water To convert moles intg number of molecules, mass or volume and vice versa simply follow the scheme below. ‘Nati ‘Avegaditscongnt ue ace Molec Bias Tame Fetaivo ncecior (stone ate grams — MoUs Bias —— = ‘Molar volume Fee moti [ Bale Conversion to and from molesMonosaccharides may combine together in pairs to give a disaccharide (double-sugar). The union involves the loss of a Single water molecule and is therefore a condensation reaction. ‘The bond. which is formed is called a glycosidic bond. Itis wo bey et usually formed between carbon atom 1 of one monosaccharide . and carbon atom 4 of the other, hence it is called a 1,4 glycosidic . . bond (Gee Fig, 2.2). Any two monosaccharides may be linked in : this way to form a disaccharide, of which maltose, sucrose and se lactose are the most common. 7 ‘The addition of water, under suitable conditions, is necessary civ : if the disaccharide is to be split into its constituent i : son monosaccharides, This is called hydrolysis ‘water-breakdown’ ] or, more accurately, ‘breakdown by water’. 1 Disaccharides, like monosaccharides, are sweet, solubleand =F crystalline. Maltose and lactose are reducing sugars, whereas sucrose is a non-reducing sugar. The significance of this is considered in Section 25.5 vee i rseoricy AS. « 4 CtwegRe ee. ‘Sucrose, fe ih 6 7 i eee eet ‘ oO i = Gipmc bene Cv ee bab ‘ i ‘The removal of ater (condensation) from the rio Irom groups OF) on carbons Tard ofthe respective ghicose Inoleculesforins ¢mliose niléeule, Som carbon and liydrogen athe have been onied for srl. Sterseisformed by acondentato eactonbervernne 5 singled. Fig. 2.2 Formatiox of maltose and sucfose :‘Stare ana glycogen ane degraded i the lgestive tract by cnanyiast, Branylase end auylo-a-{1—6)- glucosidase Amylase san endglucosidase eich raomly Inydrolyses (1 A) linkage of the side chains of glycogen ‘ad annglopctin, tt enn clnoe ether side ofa ranch point excep in very highly branched regions p-Amylasean nye soueily ences Pnatese fo the edo th oer roles ut tops tong bere ary bral pos are rence. “The structures eemaining ar hydrolysis by ce aud ‘Beamylase recalled lint dextrin and comprise about tee daze glucose ees. Amylo-e-{1— 6}. glucosidase; the debrmiching zyme, ciyses the hyprolysis ofthe 16) yeas bands of. the init dextrins, hereby penning ftir Ereakdoun by cand B-amyiose Sono railed 3, Compare the'starch grains frorn both. types of seed, : In the same way that two monosaccharides may combine in pairs to give a disaccharide, many monosaccharides may ‘combine by condensation reactions to give a polysaccharide. The number of monosaccharides that combine is variable, and the chain produced can be branched or unbranched. The chains may be folded, thus making them compact and therefore ideal for storage. The size of the molecule makes them insoluble — another feature which suits them for storage as they exert no osmotic influence and do not easily diffuse out of the cell. Upon hydrolysis, polysaccharides can be converted to their constituent monosaccharides ready for use as respiratory substrates, Starch and glycogen are examples of storage polysaccharides, Not all polysaccharides are used for storage; cellulose, for example, is a structural polysaccharide giving, strength and support to cell walls 25.1 Starch Starch is a polysaccharide which is found in most parts of the plant in the form of small granules. It isa reserve food formed from any excess glucose produced during photosynthesis. It is common in the seeds of some plants, e.g. maize, where it forms the food supply for germination. Indirectly these starch stores form an important food supply for animals. Starch is a mixture of two substances: amylose and amylopectin. Starches differ slightly from one plant species to the next, but on the whole they comprise 20% amylose, 79% amylopectin, and 1% of other substances such as phosphates and fatty acids. A comparison of amylose and amylopectin is given in Fig, 23. 25.2 Glycogen Glycogen is the major polysaccharide storage material in animals and fungi and is often called ‘animal starciy. It is stored mainly in the liver and muscles. Like starch it is made up of e-glucose molecules and exists as granules. Itis similar to amylopectin in structure but ithas shorter chains (10-20 glucose units) and is, more highly branched. 2.5.3 Cellulose Cellulose typically comprises up to 50% of a plant cell wall, and in cotton it makes up 90%, Itis a polymer of around 10000 B-ghucase molecules forming a long unbranched chain, Many chains run parallel to each other and have cross linkages between them (Fig. 2.4), These help to give cellulose its considerable stability which makes ita valuable structural material. The stability of cellulose makes it difficult to digest and therefore not such a valuable food source to animals, which only rarely produce cellulose-digesting enzymes. Some, however, have formed symbiotic relationships with organisms which can digest 7 cellulose. To these organisms itis the major component of theirfi i ‘athe deep Be win fon ze | Stans sco pre wt icin Fala otc mass wn io £0 085 é : ‘ala lec ase up S00 O06 20-000 gos urate Unbrarchednesealeran STRUCTURE OF MOLECULE. 1} xalycosioe sono 7 ° | —— : HOH OOH Gy ‘HoH \ {A GLyCOS0I6 BOND : ar & & a | ci “ fh Li : ° ° ©: { : Ee . saLvcosi0€ BOND { Fig. 2.3. Comparison of the properties and structures of amylase and amylopectin | } ‘ diet, Cellulose’s structural stiength has long been recognized by : humans. Cotton is used in the manufacture of fabrics. Rayon is produced from cellulose extracted from wood and its remarkable tensile strength makes it especially useful in the manufacture of tyre cords. Cellophane, used in packaging, and } celluloid, used in photographic film, are also cellulose derivatives. Paper is perhaps the best known cellulose product. etigLompoted of feglucose nits, techn nl that of Sepledepesetten ftw arangmet of gree arch, hat adjacent gucare molecules rated by 180° This eet fame bree loos! POOS0OPOOT LOSS OO POD ren Ne ete ans ha peooece pope peceeeeres: is Jvetelloe ite strctval sabi * POOOPESO PO BESO PSOE? bain e 7 HOOPOE OOO OO POT OPOO foalh TARLE23 Carbohydrates and their functions MOLECULAR ORGANIZATION 2.5.4 Other polysaccharides (Chitin Chemically and structurally chitin resembles cellulose. It differs in possessing an acetyl-amino group (NKLOCCH,) instead of one of the hydroxyl (—OH) groups. Like cellulose it has a structural function and is a major component of the ‘exoskeleton of insects and crustacea. It s also found in fungal cell walls, Bean formed sugarin | fad Such mayibe used as areapiraiory recedes Nay ore sale steictiiral oppor toe alec ards BNA sod DNA. ‘Constituent of hyeirogen carters such as NAD, NADP and FADS is “Constinene oF ATC “| Ketese sigar ‘Casbon diovide acceptor in photosynthesis Aldoie eget ‘joc eopratrysubsate in plantsand animals Syathesi of dinecherdes and poyenehnides Constant estar Galactose [Aldor eat Respachy bate Syhesisoflacone = © [Mannose Aldo roger Respirioy substrate Paice Kets oer "Respittory cuba Syndr of iain Cnsvent of ectar, Secten ts to aac imal oid ved depegal Dieses | Sucre ‘lucoses fete | Respmany sata Form in which mont arbohy deseo tergpored in plans Storage tel in some plans eg ‘Alan sien) Tacose ‘lacs galactne | Bospiaory substrate Mammalian milk conaine57 Inco, ; : thettre naj etchant sure for ecg - i Phmtose = | oinciergcone | Respiatoryoubeiale z Teta TAGES | a [ummaeiee | Map eompt catetyinae bp — ‘Aanylopectin | S| ccglucose with " Taye inks tranche chin of telus isi | ean is gtyenite fine ‘Gyeogen Highly branded chor | Majr rage carbohydrate in animal an fog [cs of gluse ih yo : ne Celltee Gnbranched dainot | Giiessiracheal sippor tel wall Plucis wis th Ta physi las : comtridges ‘ein CGrbranched din | Miler stoage erbohydetein some plans og, Jerwslen oftratore wath richle; Die 12 pyeoslinis chien ‘Untrancied chain ot | Contuent ofthe excoelion of ints nd rstacza Pracetylglucosamine uurits with 14 glycosidic Tinks cibiasinin tirennionsiuarsTADLE24 Relationship between amount of reducing sugar and colour of precipitate on boi ‘with Benedict's ceagent ‘Thelireeteitvcerides may al the sme, thereby forming aainpletrighoeride,orthey maybe diferent im which fase mixed Wrilycoride i proved. In eter cose iis ondenstion rentlon Fig. 2.5 Formation of a triglyceride \ ay Inulin.~ Thisis a polymer of fructose found as a storage carbohydrate in some plants, e.g. Dalila root tubers. Mucopolysaccharides ~ This group includes hyaluronic acid, which forms part of the matrix of vertebrate connective tissues. It is found in cartilage, bones, the vitreous humour of the eye and synovial fluid. The anticoagulant heparin is also a member of this group of polysaccharides, 2.5.5 Reducing and non-reducing sugars All monosaccharides, whethei aldo- or keto-sugars, are capable of reducing copper (Il) sulphate in Benedict's reagent to copper ( oxide (see Table 2.4). When monosaccharides combine to form disaccharides this reducing ability is often retained with the sesult that sugars such as lactose and maltose, although isacchazides, are still reducing sugars. In a few cases, however, {the formation of a disaccharide results in the loss of this, reducing ability. This is true of the formation of sucrose which is ierefore a non-reducing sugar. Lipids are a large and varied group of organic compounds. Like carbohydrates, they contain carbon, hydrogen and oxygen, although the proportion of oxygen is much smaller in lipids. They are insoluble in water but dissolve readily in organic solvents such as acetone, algohols and others. They are of two types: fats and oils. There is no basic difference between these ‘wo; fats are simply solid at room temperatures (10-20°C) whereas oils are liquid. The chemistry of lipids is very varied but they are all esters of fatty acids and an alcohol, of which glycerol is by far the most abundant. Glycerol has three hydroxyl (OH) groups and each may combine by means of an ester bond, with a separate fatty acid, forming a triglyceride (Fig, 2.5). [tis a condensation reaction and thus hydrolysis of the triglyceride will yield glycerol and three fatty acids. cng goe—ramcat ] noe —[ Faas ; | Tavae [+ too —[ ramaaee] v0 “| ayaa] bupoc—[ Favaaas Dyed oe Stata = Tentin gS 26:1 Fatty acids ‘As most naturally occurring lipics contain the same alcohol, namely glycerol, itis the nature of the fatty acids which determines the characteristics of any particular fat, All fatty acidsdouble bonds in which case it is said to be unsaturated. If, however, it possesses no double bonds itis said to be saturated. Itcan be seen from Table 2.5 that the hydrocarbon chains may ‘be very Jong. Within the fat they form long ‘tails’ which extend from the glycerol molecule. These ‘tails’ are hydrophobic, ie. , they repel water, ‘TABLE2S Natureand accurzence of some fatty acide ‘Alfa | Animal and ‘engetable fats - ‘Animal ane ‘vegetable fats Ardiidie | Gab,coott | Saturated Peanut oil Ceratic CeHACOOH | Satureted Wool sit contain a carboxyl group (—COOH). The remainder of the .- ; molecule is a hydrocarbor'chain of varying length (examples * are given in Table 2.5). This chain may posseds one or more \ 2.6.2 Phospholipids i Phospholipids are lipids in which one of the fatty acid groups is I / replaced by phosphoric acid (H,PO,) (Fig. 2.6). The phosphoric | { acid is hydrophilic (attracts water) in contrast to the remainder i ! _ of the molecule which is hydrophobic (repels water). Having a one end of the phospholipid aitracting water while the other end i repels it affects its role in the cell membrane. : ; e¥jcoo— fatyeat + Leng eh yeas | Fy oct ete | rl Fig. 2.6 Structure of a phospholipid 2.6.3 Waxes ‘Waxes are formed by combination of fatty acids with an alcohol other than glycerol. This alcohol is much larger than glycerol, / and therefore waxes have a more complex chemical structure. ‘Their main role is in waterproofing plants and animals, although i they form storage compounds in a few organisms, eg. castor oil and in fish. | a sresimaccnsssiDh i i2.64 Functions of lipids, + 1. An energy source - Upon breakdown they yield 38kj g~! of energy. This compares favourably with carbohydrates which Yield 17 kJ g~“and means lipids are excellent energy stores. This makes them especially useful for animals where locomotion requires mass to'be kept to a minimum. In plants they are useful in seeds where dispersal by wind or insects makes small mass a necessity. This explains the abundance of ois extracted from seeds and fruits, e.g, olive, linseed, castor, peanut, coconut and sunflower. Their insolubility is another advantage, as they are not easily dissolved out of cells, ‘ 2. Insulation ~ Fats conduct heat only slowly and so are useful insulators. In endothermic animals, such As mammals, fat if | stored beneath the skin (subcutaneous fat) where it helps to retain body heat. In aquatic mammals, such as whales, seals and manatees, hair is ineffective as an insulator becauise it cannot } trap.water in the same way as it can air. These animals therefore ‘have extremely thick subcutaneous fat, called blubbet, which | forms an effective insulator. | 3. Protection - Another secondary use to which stored fat is put is as a packing material around delicate organs. Fat surrounding the kidneys, for instance, helps to protect them from physical damage. j 4, Buoyancy ~ Being less dense than water, lipids aid buoyancy} of aquatic vertebrates such as sharks, seals and whales. Sharks have extremely fatty livers which make up to 25% of their body volume and contain a lipid, squaline, with a specific gravity of only 0.86. Oils on bird feathers are especially important in \ keeping aquatic varieties‘afloat, 5. Waterproofing ~ Terrestrial plants and animals have a need to.consetve water, Animal skins produce oil secretions, e.g. from the sebaceous glands in mammals, which waterproof the body. ‘ Cils also coat the fur, helping to repel water which would otherwise wet it and reduce its effectiveness as an insulator, Birds spread oil over their feathers, from a special gland near the cloaca, for the same purpose. Insects have a waxy cuticle to prevent evaporative loss in the same way that plant leaves have one to reduce transpiration. 6. Cell membranes — Phospholipids are major com \ponents of the cell membrane and contribute to many ofits properties (see Section 4.2.2). ’ : 7. Other functions ~ Lipids perform a host of miscellaneous functions in different organisms, For example, plant scents are fatty acid (6r their derivatives) and so aid the attraction af insects for pollination: Bees use wax in constructing their honeycombs, : 2.6.5 Steroids I Steroids are'related to lipids, and cholesterol is perhaps the best known. It is found in animals where itis itnportant in the synthesis of steroid hormones, such as vestrogen and cortisone.TS. human aorta with a fatty alteroma ly obstueting the interior a MOLECULAR ORGANZA © proteins and without wabtifig etergy counters jeakage, Cholesterol is an important constituent of myelin and ‘helps to prevent the outward flow of ions which would “shor ‘ciredit’ the ihovement of netve-imipulses along the axon, second role of cholésterol in membranes is to pull together the {gtty acid chains in phospholipids, restricting their movement, but nol making thént solid: Cholesterol is also used by. the liver for making bile salts and, in small quantities, is ysed fo make steroids in the ovaries, testes and adrenal glands. In total the body contains a pool of about 120-150 g of cholesterol which is maintained by biosynthesis in the liver and intestine and by ingestion of meat, seafood, eggs and: dairy produce. Vegans take in no cholesterol but most ather iets result in an intake of approximately 0.5g, the body making a further 0.5 g,,per day. Cholesterol is lost from the body mainly as ble salts, but also as bile, in cells from the lining of the intestine and a tiny percentage as steroid hormones in the urine. _ Cholesterol is insoluble in water but can be carried in the blood plasma in the form of lipoproteins. The balance of these lipoproteins is usually maintained by special receptors in the liver cells but saturated fats in the diet decrease their activity ‘and hence lead to a rise in plasma cholesterol. Deposits of crystalline cholesterol and droplets of cholesterol esters can cause thickening of the artery walls (atherosclerosis). This can lead to heart attacks (from blocking of coronary atteries), strokes (brain arteries blocked) or blockages of arteries in the legs. Atherosclerosis may follow damage caused to the artery walls by high blood pressure and smoking. Smoking considerably decreases the concentration of the antioxidant vitamins E and C in the blood resulting in the oxidation of some lipoproteins, t ‘The products of oxidation are oftén toxic to the cells of the artery and cause them to behave abnormally. The damaged cells release substances which cause the blood to clot and the artery to contract. Macophages which degrade the oxidized lipoproteins are unable to deal with the cholesterol it cazties. Eventually they fill with cholesterol and die, depositing the cholesterol back into the artery. Other important steroids include vitamin D and bile acids.Proteins are organic compounds of large molecular mass (up to 40.000 000 for some viral proteins but more typicallly several thousand, e.g. haemoglobin = 64500). They are no! truly soluble in water, but fotm colloidal suspensions, In addition to carbon, hydrogen and oxygen, they always contain nitrogen, usually sulphur and sometimes phdsphoriss. Whereas there are relatively few carbohydrates and fats, the number of proteins is almost limitless. A simple bacterium such as Escherichia coli has around 800, and humans have over 10000. They are specific to: ‘each species. Glucose is glucose in whatever organism it occurs, but proteins vary from one species to another, Indeed, it is the ‘proteins rather than the fats or carbohydrates that determine the characteristics of a species: Proteins are rarely stored in organisms, except in eggs or seeds where they are used to form the new tissue. The word protein (from the Greek) means ‘of first importance’ and was coined by a Dutch chemist, Mulder. ‘becatise he thought they played a fundamental role in cells. We now know that proteins form the structural basis of al: living cells'and that Mulder’s judgement was sound. 2.7.1 Amino acids . Amino acids are a group of over a hundred chemicals of which around 20 commonly occur in proteins. They always contain a basic group, the amino group (—NH,), and an acid group, the carboxyl group (-COOH). (See Fig. 2.7.) Most amino acids have one of each group and are therefore neutral, but a few have more amino groups than carboxyl ones (basic amino acids) while others have more carboxyl than amino groups (acidic amino acids), Histidine and arginine are examples of basic amino acids; aspartic acid and glutamic acid are examples of acidic amino acids. Amino acids are soluble in water where they form ions. ‘These fons are formed by the loss-of a hydrogen atom from the ciirboxyl group, making itnegatively charged. This hydrogen atom associates with the amino group, making it positively charged. The ion is therefore dipolar— having a positive and a ' negative pole. Such ions are called zwitterions (see Fig. 2.8). Amino acids therefore have oth acidic and basic properties, i.e. they are amphoteric. Being amphoteric means that amino acids act a5 buffer puiuiius buffer sului one which resists the tendency-to alter its pH even when small amounts of acid or alkali are added.to it. Such a property is essential in biological systems where any sudden change in pH could adversely affect the performance of enzymes.Where conte nore (han or earboxy rau (Fie ein a sparc Fig. 2.7 Structure of a range of wmino acids The nysrogan tom siesonstesro Inecaboat som ane ‘sco wih, theaino oun, ‘Te amo groups 4 nin esha aed Me 1 R-o—H d The con gone oF No- negatively hare Fig. 2.8 Zreillerion formation in amino acits Whorefiae Iyracbsn chal Meehan — hyaroceson tng Beste stuctre ot nario acid } isin au (bse). (COO earn run cde) 4 i any one of svat) t ‘letamiea srvces Where Reoniaing 4 or ‘ere R ontans more than ena amine gous Sbosipamino ase 2.7.2 Formation of polypeptides We have seen that mortosaccharicies may be linked to form disaccharides and polysaccharides by the loss of water (condensation reaction), Similarly, fats are formed from. condensation reactions between fatty acids and glycerol. The formation of polypeptides follows the same pattern. A conclensation reaction occurs between the amino group of one amino acid and the carboxy! group of another, to form a dipeptide (see Fig, 2.9), Further combinations of this type extend the length of the chain to form a polypeptide (see Fig. 2.10). A polypeptide usually contains many hundreds of amino acids. Polypeptides may be linked by forces such as disulphide bridges to give proteins comprising thousands of amino acids. 2.7.3 Structure of polypeptides ‘The chains of amino acids which make up a polypeptide have a specific three-dimensional shape. This shape is important in the functioning of proteins, especially enzymes. The shape of a polypeptide molecule is due to four types of bonding which occur between various amino acids in the chain (see Fig. 2.11). The first type of bond is called a disulphide bond. IE arises between sulphur-containing groups on any two cysteine molecules, These bonds may arise between eysteine molecules in the same amino acid chain (intrachain) or between molecules in different chains (interchain).PARTI PA mn, NOTEBOOK Electrophoresis, ‘The second type of bond is the ionic bond. We have seen that amino acids form 2witterions (Section 2.7.1) which have NH,* and COO™ groups. The formation of peptide bonds when making @ polypeptide means that the COOH and NH, groups are not available to form ions. In the case of acidic amino acids, however, there are additional COOH groups which may ionize to give COO™ groups. In the same way, basic amino acids may still retain NH,” groups even when combined into the structure Electrophoresis is a technique used to separate molecules of different electrical charge. Under the intiuence of an electrical fleld, anions (negatively charged ions) will move towards the anode (positive electrode) while cations (positively charged ions) are attracted to the cathode (negative electrode). 3 te anode JexHo0e ‘Two factors affect the speed with which charged molecules move towards an electrode: 1. The amount of charge — the greater the charge the faster the molecule moves. 2. The size of the molecule ~ small molecules move faster than larger ones with the same charge. : Amino acids and proteins are amphoteric (have both basic and acidic properties) because they are zwitterions (have postively and negatively charged groups). ‘The amount of positive or negative charge is affected by pH. Each molecule has a specific pH at which the total positive charge is exactly equal to the total negative charga, i, itis electrically neutral and has no tendeney to move to either the anode or cathode of an electric field. This is known as the isoelectric point. At higher pH protein and amino acid molecules become more negatively charged while at lower pH they become more positively charged. i i |: MOLECULAR ORGANIZAHON: MOLECULAR ORGANTA Typical apparatus for carrying out ofa polypeptide. In addition NH," and COO- can occur at the erids of a polypeptide chain. Any of these available NH," and COO groups may form ionic bonds which help to give a ‘polypeptide molecule its particular shape. These ionic bonds are ‘weak and may be broken by alterations in the pH of the medium -around the polypeptide. ! ‘The third type of bond is the hydrogen bond. This occurs between certain hydrogen atoms and certain oxygen atoms ‘The ano old becomes ‘mecenagelvaly charge ands harotreataciod ‘othe anna, ‘The molecules being separated have to be supported in an appropriate medium such as paper or a thin layer of gel, Either end of a strip of the medium is dipped in a small reservoir ‘of buffer solution of the appropriate pH. Each reservoir also contains an electrode. The electrical field is applied for a specific period of time and then the position of the molecules is determined by adding a suitable ~ stain.to colour them. The molecules are separated according to theit charges; the negatively charged ones moving to the anode with the ‘most negatively charged ones moving furthest. The positively ‘charged ones move to the cathode and again the more positive they are the closer they get to the cathode, Itis possible to treat the mixture being separated in such a way that allthe molecules are equally negatively charged. These can then be loaded at the cathode end of the apparatus and will bs attracted to:the anode. The distance they travel in a given time wil ‘then depend not on their charge but their size, the smaller molecules moving further than the larger ones, Skip of wire of motes Bute spin of ANODE pape is pied ai pant ‘ppropring pH. CATHODE: + Steel ealed Ba ergy SOOT. { suppon o tat stp ‘Fig. 2.10 Formation of a polypeptide - A ad repreettatidn ofa polynentide chain to show. {have perf bonding respon for shaping the chan tn locice he pole chetn re lege, con mir f= these tre typeraf bd ond havea tree mensional shape ¥en ene mac : $5. ecoo-in ‘Soup . oe |eoinet bon: son Fig. 211 Types of bond ina polypeptide chain £8 Selanne tie-in ropa > ‘ese cihe 2 or 00 us omen ta ly cougar Fig. 2.9 Formation ofa dipeptide within the polypeptide chain. The hydrogen atoms have a small positive charge on them (electropositive) and the oxygen atoms a ‘small negative charge (electronegative). The two charged atoms are attracted together and form a hydrogen bond. While each bond is verytweak, the sheer number of bonds means that they play @ considerable role in the shape and stability of a fe polypeptide iolecule. ‘The fourth type is hydrophobic interactions which are interactions between non-polar R groups. These cause the protein to fold as hydrophobic side groups are shielded from water. 2.74 Fibrous proteins The fibrous proteins have a primary structure of regular, repetitive sequences. They form long chains which may run parallel to one another, being linked by cross bridges. They are very stable molectiles and have structural roles within organisms. Collagen (Fig, 2.12) is a good example. Itis a common constituent of animal connective tissue, especially in structures requiring physical strength, eg. tendons. It has a primary structure which is largely a repeat of the tripeptide sequence glycine-proline-alanine, and forms a long unbranched chain. Three such chains are wound into a triple helix, with cross bridges linking them to each other and providing additional © structural support. (Compare the repeating glucose units, parallel chains and cross links of the structural carbohydrate cellulose.) 2.75 Globular proteins In contrast to fibrous proteins, the globular proteins such as insulin have highly isregular sequences of amino acids in their : «Bolypeptide chains, Their shape is also different, being compact Blobules. {fa fibrous protein is likened to a series of strands of sizing twisted into a rope, then.a globular protein can be thought © of as the same string rolled into a ball (see Fig, 2.13). These: molecules are farless stable and have metabolic roles within organisms. All enzymes are globular proteins. Globular and fibrous, proteins are compared in Table 2.6. esas SERRE stMOLECULAR onc ANZA ee Fig. 2.12 Fine structure of the fibrous protein: collagen course truly permanent, The hai hair has the same disulphide 2.7.6 Conjugated protéins Many proteins incorporate other chemicals within their structure, These proteins are called conjugated proteins and the non-protein part is referted to as the prosthetic group. The prosthetic group plays a vital role in the functioning of the protein, Some examples are given in Table 2.7. A ingle clagen fixe a eenin fe econ a cctaen meet ace up of ricoscope. Each ibroccnare afew ves poypapice cha wound thousand eotapon cuts. so tip ale Cologentives tings i ong rato connective teu, Megafeaten’ 7009000 p01)(0) The sec sicar site itape lich he pide lala fomer sg ocrogen bonding. This most fet a spire big aD fl al configurations occur, ied y (4).Thequiternary stencture cise fro the cdmbbion of a mane of diferent polypeptide chain, and associated non poten gon into large eamples prc molec sop Potpeetce holed Ral fy unleaewere Solubléforiis colloidal stependions Meiueme OS Tap sche al auyen io henge :“Details ofthe molecular structure of haemoglobin are given in Section 2.21, i 2.7.7 Denaturation of proteins We have seen that the three-dimensional structure of a protei is, in part at least, due to fairly weak ionic and hydrogen bonds. Computer gral : Any agent which breaks these bonds will cause the three- termalysine dimensional shape to be changed. In many cases the globular proteins revert to a more fibrous form. This process is called denaturation. The actual sequence of amino acids is unaltered; only the overall shape of the molecule is changed. This is still sufficient to prevent the molecule from carrying out its usual functions within ai organism. Denaturation may be temporary or perinanent ani variety of factors as shown in Tabie 2.8. due toa ‘TABLE 28 Factors causing protein denatur J] Bample ‘Causes the atoms of the proiein to vibrate: more" ‘Coagulation of albumen (bat (eee vee gery sikh | oe a at oi fonigbonds : : “Additional H’ ions in acids combine with COO™ ‘The gouring of milk by acid (eg, Laclbeclus batter, ; groups.on amind aids and form’ COOH. Fonicbouds | prodiices lactic acid, lowering pH and causing ite ! ase hence broken denature the casein, making itinsaluble and thus =} forming cutds) 3 ‘Alalls Reduced number of H ions causes NH," groupe to ose : S : |’ lois a orn NH, Ionic boris se hence broken | Seo Tespulctiviels | Thclorsol heavy vie ouch a ooury andl ‘Many Stays ae lahniea fy bong denérarel nie oe | highly electropostiv. They combine with COO | presence ofcertnn ions eg. ejtochrome oxidase groups ond disrapionic bands, Silly, highly. | (tespieaocy enzyme) is inhibited by cyanide stecronegtve ions og. janide N=) cain with : ee NI" groups and disrupt onic bonds : : | ‘Organic diemjeals | Organ solveni lier hydrogen bonding withina., - | Alcohol ceatureecerain bacevalprofeins. Thies S| protein ‘whut iakesituseful or sterizaton : | RERRRISr Eo |apuel enter bee ipo ‘Strething 3 hair breaks the hydeogen bonds i he Keratin helix The eli extendec ac the hair eid Ifreleased, the hair retuéns to is normal length hhawever iis wetted and then deed anes tensi Heep its ae lengl- ie bass of hair yngPART TASLE29 Fenctions of proteins ‘a ‘fotiiil lo the delenee of te Body; e.g agaliat tact Growth ‘Contras growth and inetebolisrh y ae “Bxereton Catalyse feactions in ornithine cycle and therefore help in protein breakdown and urea formation ‘Nested for ele contmision g ‘Fadiiitain Omen Svctual support ln vba na a [olen pos aa Tea vita ta age d | Gives strength and slesticity to ligaments 7 ere ‘Tough for protection eg natal cays, nals Hoge akin fee seleratin” Fs Provides strength in insect exoskeleton. © flippers Sitti compen al el eras Sense ad | Horo ug insula” | Contol lod ugarieyel :Seounater | sewescenceuopitchomnone:| Contac heasttry ate sarenlciiex <= a Sp apoprestin = 802 "Canbis bloc preahuns ae Rhodopsin/opsin Phytachramea! 6 Visual pigments inthe retin, aenaltive to light ~ | Plant pigments inpovtat in omit of oeeing Harnosolen pb 2 | asa preci nal truchitel support to divoihosomes \ Storade protein in seeds ~nburishes the embryo NCCE oi and anders whic ina be ue for sesil dipley: es 28 Nuicleic acids : nee Liké proteins, nucleic acids are informational macromolecules. ‘They are made up of chains of incuvidual wuts called nucleotides. The structure of nucleic acids and their constituent nucleotides are closely related to their functions in heredity and protein synthesis. For this reason the details of their structure will be left until the nature of the genetic code is discussed in Chapter 7.human diet. Copy and complete the tablet ‘one physiclogical function in humans of ea¢ in the spaces provided: ae Nitin [ Oiephysiolopeat aca (@) Describe the differences in molecular structure between cellulose and starch, S (2 marks) Cellulose has a structural function in plants while starch has a storage function. (b) Relate these functional differences to the differences in molecular structure of cellulose and starch. + (4 marks) {c) Name the bond formed between adjacent glucose molecules in starch and cellulose. * (1 mark) (d) Suggest why amylase, the enzyme that catalyses the hydrolysis of starch, will not catalyse the hydrolysis of cellulose. (2 marks) (Total 9 marks) UCLES June 1996, Paper 3, No. 2 2, The table below refers to two organic molecules. Copy the table. If the statement is correct for the molecule, place a tick (7) in the appropriate box. If it is incorrect, place a cross (X) in the appropiate box. Statement ‘Triglyceride [Glycogen ‘Contains only carbon, Cali Toa ‘ ‘Phosphate 3 ‘Nicotinic acd (Total 4 marks), Esdexcel June 1998, B2, No. 1 4. The diagram below shows the structure of a lipid molecule. yg 7 = (@) (i) Name the parts labelled A and B. (2 marks) (ii) Name this type of lipid. (mark) (i) Name the chemical zeaction used to form the bonds between A and B. (L mark) (@) Gi) State one function of this type of lipid in living organisms, (mark) (ii) State one feature of the molecules of this type of lipid which makes them suitable for the function you have, given. (mark) (Total 6 marks) Erexcel June 1997, BIFIBI, No. 2 5. The statements in the table below refer to three polysaccharide molecules. Copy and complete the table. Ifthe statement is corzect, place a tick (¥/) in the appropriate box and if the statement is incorrect, place a cross (X) in the appropriate box. Edexcel june 1998, B/HB1, No. 3 hydrogen and oxygen ‘Glycosidic bonds present Statement Starch | Glycogen | Cellulose Sclibe in water Polymer of glucose Provides storage of energy Glycosidic bonds present [Occurs in flowering plants, Unbranched chains only ane animes, Energy store in animal cells (Total 5 marks) (Total 4 marks) Edexcel june 1997, B[HEBL, No. 4‘protein synthesis, - @) What is the name given to this bond? ae oeeiean Cmarky = 1G). Copy the diagrams and putia ming {around the atoms which ate femove when A and B are joined together. ee) rraw-atline connecting the atoms in _Aand Bwhich are bonded, “(1 mark) (G) Describe how the properties of the side groups R, and R, may vary, and liow these are involved in the structure of proteins, (4 marks) (@ Copy and complete the table below giving a named example ofa protein having the function indicated, (This diagram represents a sinall polypeptide Onsisting of eight amin acids, sz, wala Of thé cherhical group, : ippear at the end of HG arh ype of reaction by which ee joined together. (1 mark) gent or feagents you est for the presence of a nak) . = Total 6 marks) cs tity 1997, Paper BYOL, No. 1 Mra Funetion Example of protein ‘Contractile Enzymie Transport Strucairal ‘Hormone Protéction from disease! 07°: = marks) (Total 11 marks) Orford june 1997, Paper 1, No.2 7. « (a) Copy and-compiete the following table with ticks (7) to show which properties apply to each biochemical com, Blchenicaleompound Propeny Menosccarde | stares | Cattse | tipit | Pia Iga polymer Contin toge ee ‘ssohble in water I | (marks) (2) Suggest a suitable name for each structure, AD, (4 marks) (©) Given that the chemical forma for ghuicose 18 CHO, write down the equation to show the production of the disaccharide maltose. 2 marks) (0) Briefly explain how you could distinguish, using a practical teclinique, between tha Presence of a reducing sugar, such as maltose, and a non-reducing sugar, suchas sucrose, (3 marks) (Total 9 marks) Osford February 1997, Paper 1, No“The catalytic amino acids A, B and C,althongh some distance apart in the clin, are close together then the protein is flied Fig. 3.1 Catalytic amino acids forming the i active site Until zecently it was thought that all biological catalysts were enzymes. We now know that other substances may carry out catalytic finctions in living organisms. Abzymes are antibodies with catalytic properties and ribozymes are molecules of RNA which act catalytically on themselves. Most biological catalysts however are globular proteins known as enzymes. A catalyst is a substance which alters the rate of a chemical reaction without itself undergoing a permanent change. As they are not altered by the reactions they catalyse, enzymes can be used over and over again. They are therefore effective in very small amounts. Enzymes cannot cause reactions to occur;-they can only speed up reactions that would otherwise take place extremely sipwly. The word ‘enzyme’ means ‘in yeast, and was used because they ‘were first discovered by Eduard Buchner in an extract of yeast. Enzyme structure and function Enzymes are complex three-dimensional globular proteins, some of which have other associated molecules. While the enzyme molecule is normally larger than the substrate molecule it acts ‘upon, only a small part of the enzyme moleculé actually comes into contact with the substrate. This region is called the active site. Only a few of the amino acids of the enzyme molecule make up the active site. These so-called catalytic amino acids are often some distance apart in the protein chain but are brought into close proximity by the folding of that chain (see Fig. 3.1). ‘Amina aid cin lees i rayne cctgraion- Enaepy boi wate Energy bie sib enayra Energy level debate 2 5 Tia eving recto Fig. 3.2 Hod citzynnes lower the activation * energy‘ ‘bitte inant’ aye + suiscate > Emayme-statecomplst ——————® nays + products Fig, 3.3 Mechanisn: of enzyme action 3.1.1 Enzymes and activation energy Before a reaction can take place it must overcome an. energy barrier by exceeding its activation energy. Enzymes‘operale by lowering this activation energy and thus permit the reaction to ‘occur mate readily (Fig. 32).-As heat is often the source of activation énergy, enzymes often dispense with the need for this heat and so allow reactions to take place at lower temperatures. Many reactions which would not ordinarily occur at the temperature of an organism do so readily in the presence of enzymes. 3.1.2 Mechanism of enzyme action f Enzymes are thought to operate on a lock and key mechanism. In the same way that a key fits a lock very precisely, so the substrate_fits accurately into the active site of the enzyme molecule. The two molecules form a temporary structure called the enzyme~substrate complex. The products have a different shape from the substrate and so, once formed, they escape from «the active site, leaving it free to become attached to another substrate molecule, The sequence is summarized in Fig, 3.3. Produ moles patve ste Fre acoot nator sstate rena Eyre reo ‘Modern interpretations of the lock and key mechanism suggest that in the presence of the substrate the active site may change in order to suit the substrate's shape, The enzyme is flexible and moulds to fit the substrate molecule in the same i way that clothing is flexible and can mould itself to fit the shape of the wearer, The enzyme initially has a binding configuration which attracts the substrate. On binding to the enzyme, the stibstrate disturbs the shape of the enzyme and causes it to assume a new configuration, Itis this new configuration that is catalytically active and affects the shape of the substrate, thus lowering its activation energy. This is, referred to as an induced fit of the substrate to the enzyme. ieotaeA+B“ C+D carbonic anbydense im CO, +H,0 ——> H,CO, cexrbonic anhydrase H,CO, ——> CO, + H,0 (in the lungs) (in tissues) ities ecess sunsraie he Fee of ance: contnos 0 tie amount i fubevale seies ‘he gaphiais ol) Pate of reacton i. Vetcty [I Enayrecansenvation Fig. 3.4 Graphs to show the effect of eizyrme concentration on the rate of an-enzyme- controlled reaction The properties of enzymes can be explained in relation'to the lock and. key mechanism of enzyme action, and the theory of induced fit. 3.2. Specificity Allenzymes operate only on specific substrates. Just as a key has a specific shape and therefore fits only complementary locks, so only substrates of a particular shape will it the active site of an enzyme. Some locks are highly specific and can only be opened with a single key. Others are opened by a number of similar keys; yet others may be opened by many different keys. In the same way, some enzymes will act only on one particular isomer. (Others act only on similar molecules; yet others will Break a particular chemical linkage, wherever it occurs. 3.22 Reversibility Chemical reactions are reversible, and equations are therefore often represented by two arrows to indicate this reversibility. (See opposite.) , Atany one moment the reaction (shown left) may be proceeding predominantly in one direction. If, however, the conditions are changed, the direction may be reversed. It may be that the reaction proceeds from left to right in acid conditions, but in alkaline conditions it goes from right to left. In time, reactions reach a point where the reactants and the product are in equilibrium with gne another. Enzymes catalyse the forward. and reverse reactions equally. They do not therefore alter the ‘equilibrium itself, only the speed at which it is reached. Carbonic anhydrase is an enzyme which catalyses a reaction in either direction depending on the conditions at the time. In respiring tissues, where there is much carbon dioxide, it converts carbon dioxide and water into carbonic acid. In the Iungs, however, the removal of carbon dioxide by diffusion means a low concentration of catbon dioxide, and hence the carbonic acid breaks down into carbon dioxide and weter. Both reactions are cataiysed by carbonic anhydrase, as shown opposite. 3.23 Enzyme concentration ‘The active site of an enzyme midy be used again and again. Enzymes therefore work efficiently at very low: concentrations. The number of substrate molecules which an enzyme can act upon in a given time is called its turnover number, This varies from many millions of substrate molecules each minute, in the case of catalase, to a few hundred per miniute for slow acting ‘enzymes. Provided the temperature and other conditions are suitable for the reaction, and provided there are excess substrate molecules, the rate of a reaction is directly proportional to the enzyme concentration. If the amount of substrate is-restricted, it may limit the rate of reaction. The addition of further enzyine cannot increase the rate and the graph therefore tails off (Fig. 3.4).Algal sos. 49 Ahan dlc 22 gs etewcebnid ‘Mesimu pig eseacion ‘Some page peel, shave alr he Hoe alenle” ‘Subaratsecnoertaian Fig. 3.5 Graph to show the effect ofsubstrate concentration arr the rate of an enzyme~ controlled reaction ave of a easton Vloaty IV > 7 o 2 © 0 w Teperanrerc 3 wich reaton creaaes ue reas tte egy ose ‘el anzyre'nelacler, + Rate al wiih eeactondecreseae 10 sanetuaton of eats noc. Actuate onc wrest th comand wet tase oo Freres ° Fig. 3.6 Graph to showo the efect of temperature ot the rate of art enzyme-controlled reaction 3.2.4 Substrate concentration | Fora giver amount of enzyme, the rate of an enzyme-controlled reaction iricreases with increasing substrate concentration ~ up to * a point. At low substrate concentrations, the active sites of the enzyme molecules are not all used ~ there simply are not enough substrate molecules to occupy them all. As the substrate concentration iricreases, more and more sites comie into use. A point is reached, however, where all sites are being used; increasing the substrate concentration further cannot therefore increase the rate of reaction, as the amount of enzyme is the limiting factor. At this point the graph tails off (Fig. 3.5). 3.2.5: Temperature An increase in temperature affects the rate of an enzyme- controlled reaction in two ways: 1. As the temperature increases, the kinetic energy of the substrate and enzyme molecules increases and so they move faster. The faster these molecules move, the more often they collide with one another and the greater the rate of reaction, 2. As the temperature increases, the more the atoms which make up the enzyme molecules vibrate. This break the hydrogen bonds and other forces which hold the molecules in their precise shape. The three-dimensional shape of the enzyme moleculds is altered to such an extent that their active sites no longer fit the substrate. The enzyme is said to be denatured and loses its catalytic properties. (See Section 2.7.7.) ‘The actual effect of temperature on the rate of reaction is the combined influence of these two factors and is illustrated in Fig. 3.6. : ‘The optimum temperature for an enzyme varies considerably. Many arctic and alpine plants have enzymes which function efficiently at temperatures around 10°C, whereas those in algae inhabiting some hot springs continue to function at temperatures around 80°C, For many enzymes the optimum temperatu‘e lies around 40°C and denaturation occurs at about 60°C. 3.2.6 pH ‘The precise three-dimensional molecular shape which is vital to the functioning of enzymes is partly the result oF hydrogen bonding, ‘These bonds may be broken by the concentration of hydrogen ions (H*) present. pH is a measure of hydrogen ion concentration. It is measured on a scale of 1-14, with pH17 being the neutral point. A pH less than 7 is acid, one greater than 7 is alkaline. By breaking the hydrogen bonds which give enzyme molecules their shape, any change in pH can effectively denature enzymes. Each enzyme works best at a particular pH, and | deviations from this optimum may result in denaturation. Fig. 3,7 illustrates the different pH optima of four enzymes. 3.2.7 Inhibition ‘The rate of enzyme-controlied reactions may be decreased by the presence of inhibitors, They are of two types: reversible inhibitors and non-reversible inhibitors.Fate of areeaton ie, Velosty 1 Fig. 3.7-Graph to show the effect of pH on the rate of reaction of four different enzynnes Fig. 3.8 Competitive inhibition 1. Inbar absen ~ ‘The substrate attaches 10 the active ste ofthe ence in the normal way. Receton takes place ax normal Inhibitor presen The inhibitor prevents tke wormal enzyne-substrate complex being formed. The reaction rate is reduce. Fig. 3.9 Noncompetitive inhibition Reversible inhibitors ‘The effect of this type of inhibitor is temporary and causes no permanent damage to the enzyme because the association of the inhibitor with the enzyme is a loose one and it can easily be removed. Removal of the inhibitor restores the activity of the: enzyme to normal, There are two types: competitive (active site-directed) and non-competitive (non-active site-directed). ‘Competitive inhibitors compete with the substrate for the active sites of enzyme molecules (Fig. 3.8). The inhibitor may have a structure which permits it to combine with the active site, While it remains bound to the active site, it prevents a substrate molecule from occupying that site and so reduces the rate of the reaction. The same quantity of product is formed, because the substrate continues to use any enzyme molecules that are unaffected by the inhibitor. It does, however, take longer to make the products. Ifthe concentration of the substrate is increased, less inhibition occurs. This is because, as the substrate and inhibitor are in direct competition, the greater the proportion of substrate molecules the greater their chance of finding the active sites, leaving fewer to be occupied by the inhibitor. ~Malonic acid is a competitive inhibitor. It competes with succinate for the active sites of succinic dehydrogenase, an important enzyme in the Krebs cycle (Section 16.3), \ ‘Subatematacle conupyng thee silo a ‘te arma Sabet soleus rable to see he ete ste Inntor rece cee tha enzyme ~ Sree vce ‘Non-competilive inhibitors attach themselves not to the active site of the enzyme but elsewhere on the enzyme molecule (Fig. 39). They alter the shape of the enzyme molecule in such a ‘way that the active site can no longer properly accommodate the substrate. As the substrate and inhibitor molecules attach to different parts of the enzyme, they argnot competing, for the ‘Sebatale aloes state moles sonupyng tha ate te sat sve ‘lie ems ‘to burnin way i ‘hat ans tha reaton z — to proceed Enyne moves shape schanged fe presance of their morale Eneye molecule raya lees Te TSsame sites. An increase in substrate concentration will not therefore reduce the effect of the inhibitor. Cyanide is a non-competitive inhibitor. It attaches itself to the copper prosthetic group of cytochrome oxidase, thereby inhibiting respiration (Section 16.4), Non-reversible inhibitors Non-reversible inhibitors leave the enzyme permanently damaged and so unable to carry out its catalytic function. Heavy metal ions such as mercury (Hg?*) and silver (Ag*) cause disulphide bonds to break. These bonds help to maintain the shape of the enzyme molecule. Once broken the enzyme molecule’s structure becomes irreversibly altered with the permanent loss of its catalytic properties. Why pH? ‘The term was frst used by the Danish biochemist S.P.L. Sérenson \when researching into the best conditions for brewing beer. Aciity is the result of free hydrogen ions (H') in a solution, The Concentration is often very low, however. Vinegar, for example, ‘ypically has a concentration of 0.001 mol dm~*. This is a rather long-winded way of expressing acid and base strength, especially when 1 M sodium hydroxide has a hycirogen ion concentration of 0.000.000000000 01 mot"S. Sérenson appreciated that 0.001 can be written as 107 and 0.000.00000000001 as 10-4, He then - simply ignored the 10 and the minus sign to give values of 3 and 14 respectively. pH is therefore the negative power (p) of the hydrogen ion concentration (H) in mol dev? 3" 40°18 10°" to" tO" 40° to 40°F t0"® 10° 10-0" G0-® ont PH i Le | |coe {A cofactor is 2 non-protein substance which is essential for sore enzymés to function efficiently. There are three types: activators, coenzymes and prosthetic groups 3.3.1 Activators ‘Activators are substances which are necessary for the functioning of certain enzymes. The enzyme thrombokinase, which converts protixombin into thrombin during blood clotting, is activated by calcium (C2) ions. In the same way Why is water neutral at pH7? ‘Some water molecules are always dissdciated into hydrogen (H*) and hydroxyl (OH™) ions: HO === Ht + OHM ‘AL25°C, 1 dm? of water contains 10-7 moles of H* fons arid tharafore has a pH of 7. It follows from the equation above that there will also be 10” moles of OH" ions. As the concentration of H* ions increases, that of OH" ions decreases corresponding. For example, ‘where thé concentration of H* ions is 10~° mol dm”® that of OH™ ions is 10~® mol dm-®, The two concentrations multiplied always give a value of 10~"*. Hence the pH scale is 0-14, At pH 0 almost allthe ions are H* whereas at pH 14 they are almost entirely OH”. The pH scale is nat linear but is logarithmic, based on a factor of 10. pH6 =0.000001 mol dm~® of H® and pS = 0.00001 mol dm™® : of H', je. pH is 10 times more acidic than pH6. In the sarne way pH Relative concentrations of H* ‘is 10 timas more acidic than pH4-and 100 times more so than pHS. ‘anal OH ions at diferent pHs. 4 ‘Sweat ie 1000¢ Water pH? roe acihan as : sregaocoot Go") esti ice pH ‘Sweat pe Wot pht7 eA REE NEL A AEA