CHEM113

BIOCHEMISTRY Transcribed by: arlene anne mendoza

Lesson 1: CELL ORGANELLES AND Ribosomes
MACROMOLECULES - Considered the cell’s protein factories
Outline - Made up of two unequal subunits, each
I. Cell Organelles and Macromolecules containing RNA.
II. Cell Organelles - Sites for the synthesis of proteins
A. Nucleus
B. Endoplasmic Reticulum Mitochondria
C. Ribosomes - largest cytoplasmic organelles and considered
D. Golgi Apparatus the cell's power plants
E. Microtubules and Microfilaments - provided with a smooth outer membrane and
F. Cell Membrane folded inner membrane, the folds called cristae
III. Cell Macromolecules
IV. Cell’s Inorganic System - synthesizes and stores energy in the form of ATP
V. Water and PH - considered as a self-regulating organelle, since
A. General Properties of Water it synthesizes its own proteins and is self-
B. Biological Importance of Water duplicating due to the presence of
C. PH Scale mitochondrial DNA and RNA
- controls concentration of water, calcium, and
CELL ORGANELLES AND MACROMOLECULES other ions in the cytoplasm; breakdown and
- In biochemistry, the different biochemical recycling of sugars, fatty acids, and amino acids
reactions associated with life will be fully
understood by taking into consideration the Golgi Apparatus
different macromolecules in relation to the
organelles of the living cell.
- flat, membranous sacs, vesicles, and vacuoles
considered as packagers of cell's proteins.
CELL ORGANELLES - responsible for concentrating and wrapping
Nucleus certain enzymes into separate organelles which
- considered as the cell's command center remain inside the cell.
- contain the genes: the units of hereditary
material. Lysosomes
- associated with very important macromolecules: - considered as the scavengers of the cells
o nucleic acids
- referred to as bags of enzymes, suicide bags, or
o deoxyribonucleic acid (DNA) of the genes
graveyard of the cell.
o ribonucleic acid (RNA) of the nucleoli
- Principal site of intracellular digestion
Endoplasmic Reticulum
- system of tubules and flattened sacs continuous Microtubules and Microfilaments
with the nuclear membrane providing the cell - Not membrane-bound
with its internal support - For transport of materials, cell movement, and
- may be in the form of: cell support
o Rough ER: associated with ribosomes on
the cytoplasmic side of the membrane and Cell Membrane
size corresponding to the quantity of - Considered as the cell’s delicate but tough
protein which cell “exports” “guardian”
o Smooth ER: without ribosomes and - Composed of lipids, proteins, and
synthesizes proteins for cell’s own use. oligosaccharides
- Regulates the translocation of materials.

CELL MACROMOLECULES
 Cell Organelles Cell Macromolecules pressure until an osmotic equilibrium is
Nucleus Nucleic acid, proteins, established. When the cell is in a medium that is
lipids hypertonic, the cell tends to shrink, while in a
Endoplasmic Reticulum Lipids, Proteins hypotonic medium, the cell tends to swell.
Ribosomes RNA, Proteins DIFFUSION - Interpenetration of molecules
Mitochondria Proteins, Lipids, CHO, between two substances occurs whenever the
nucleic acid solute distributes itself uniformly into the solvent.
Golgi Apparatus Proteins, Lipids, CHO Small molecules and ions move faster than
Lysosomes Proteins macromolecules. The rate of diffusion of
Cell Membrane Lipids, Proteins, CHO substances is dependent on the molecular size,
Microtubules & Proteins weight, shape and the concentration gradient.
Microfilaments
DIALYSIS - When a semi-permeable membrane
CELL’S INORGANIC SYSTEM allows the passage of the crystalloids but not the
- The cell (protoplasm) is a combination of true colloids, the rate of dialysis depends on the size of
and a colloidal solution since some of its the pores, temperature, electrical charge, area of
components are insoluble while others are dialyzer, and the relative concentration on the two
soluble in its water medium. sides of the membrane.
- The following are colloidal properties of the cell:
WATER AND PH
FILTERABILITY – particles of colloidal solution can - Water is an essential substance for plant and
pass through ordinary filter paper but not through animal growth.
parchment membrane.
- Without water, there would be no life on earth.
NEGLIGIBLE OSMOTIC PRESSURE – particles are
- Water is essential to life and is in solvent water
comparatively small therefore they have negligible
that the chemical reactions of biological
osmotic pressure.
processes evolved.
TYNDALL PHENOMENON – colloidal solution
- Although not an organic biomolecule, water is
possesses Tyndal Effect.
the major component of the cell, making
BROWNIAN MOVEMENT – suspended particles of a around 70 to 90% of its weight and inert space
colloidal solution are observed to be in continuous, filler in living organism.
rapid vibratory motion. - Due to its highly reactive and unusual
ELECTRICAL CHARGES – colloidal particles are properties and its ionization products H+ and
electrically charged, the charged being distributed OH-, water is an important factor in modifying
over the surface of the entire particle. structures of biomolecules such as nucleic
acids, carbohydrates, proteins, lipids, enzymes,
SURFACE TENSION – molecules in the interior of a
and other cell components
homogenous liquid are attached in all directions by
surrounding molecules so they move freely in all General Properties of Water
direction while surface molecules are attracted 1. Chemically pure water is colorless, odorless, and
more towards the center of the liquid making the tasteless.
surface molecules more compact. The force by 2. Has a higher boiling point and osmotic pressure
which the surface molecule are held is called 3. High specific heat
“surface tension.” 4. High latent heat of vaporization
5. High surface tension
OSMOSIS – whenever a semi-permeable 6. Had the capacity to dissipate heat to its
membrane separates two solutions of unequal environment.
concentrations, the fluid tends to flow from the side
of low osmotic pressure to that of higher osmotic
 Biological Importance of Water o Colligative properties depend only in the
1. A UNIVERSAL SOLVENT number of solute molecules per unit
- Water is an excellent solvent for ionic volume of solvent and independent of their
compounds because of the attraction between chemical structure.
the ionic components of the molecules and the o Dissolved solutes disturbed hydrogen
water dipoles is sufficient to overcome the bonding in water molecules, thus reducing
attraction between the ions themselves. its effect as a solvent.
- Non-ionic polar compounds are also very Water Molecule Has A Tendency to Dissociate
soluble in water. Their polar functional group - Through water ionizes slightly forming hydrogen
[OH] readily hydrogen bonds with water ion and hydroxyl ion.
molecules, dispersing the compounds among
the water molecules. pH Scale
o Sugars H+ (M) pH
o Alcohols 1.0 0
o Aldehydes 0.1 1
o Ketones 0.01 2
0.001 3 Acidic
- Other substances dispersed by water are those 1 x 10 - 4 4
hydrophobic group known as amphipathic 1 x 10 – 5 5
molecules such as salts and fat acids and are 1 x 10 – 6 6
called micelles. 1 x 10 – 7 7 Neutral
o Micelle formation is important for an 1 x 10 – 8 8
understanding of organized biological 1 x 10 – 9 9 Basic
system among amphipathic compounds
1 x 10 – 10 10
such as proteins, phospholipids and nucleic
1 x 10 – 11 11
acids.
1 x 10 – 12 12
1 x 10 – 13 13
2. AN ELECTRON DIPOLE
1 x 10 – 14 14
- Water is an irregular tetrahedron with oxygen at
its center. PHYSIOLOGICAL BUFFER SYSTEM
- Two hydrogens are bonded with oxygen forming - A system that can resist a change in pH upon the
105o a slightly skewed tetrahedron. addition of either acid or base is called a buffer.
- Because of this structure electrical charge is - Solutions of weak acids and their conjugate
not distributed uniformly about the water bases and on weak bases and their conjugate
molecule. acids exhibit buffering.
- The oxygen side is partially negative because of - Functional groups such as carboxyl group, amino
the relatively rich in electrons and the two group and phosphate esters are functional
hydrogen forming a region of local positive groups of are weak acids or bases that many
charge. biomolecules possess.
- The unequal distribution of charges with in a
INORGANIC IONS
molecule is term “dipole” such as in water.
- Vital to the normal functioning of some enzymes
3. ALTERED BY SOLUTES and for the maintenance of functional
- Colligative properties such as freezing point conformation of proteins, nucleic acids, and
and boiling point, vapor pressure and aromatic carbohydrates
pressure are altered by dissolved solutes.
 Lesson 1: Part 2 Historical Notes Eukaryotic Cell
• ROBERT HOOKE – was the first person to use - Have a membrane-bound nucleus and a
the term “cell”. He referred to the small empty number of other membrane-bound subcellular
chambers in the structure of cork as cells. (internal) organelles, each of which has a
• MATTHIAS SCHLEIDEN and THEODOR SCHWANN specific function.
– concluded that all plants and animal tissues were Plasma Membrane
composed of cells.
- Structure: Phospholipid bilayer containing
• RUDOLF VIRCHOW – proposed the theory of cholesterol and proteins and some
biogenesis where cells only arise from pre- carbohydrates; forms a selectively permeable
existing cells. boundary of the cell.
Cell Theory - Functions: Acts as a physical barrier to enclose
cell contents; regulates materials movements
• A cell is the basic structural and functional unit
into and out of the cell; functions in cell
of living organisms.
communication.
• The activity of an organism depends on the
collective activities of its cells.
• According to the principle of complementarity,
the activities of cells are dictated by their
structure (anatomy), which determines
function (physiology).
CELL
• Biochemistry explores molecular mechanisms
of normal cellular processes as well as
diseases.
Nucleus
• All higher living organism including human are
- Structure: It is enclosed within a double
made up of cells.
membrane called nuclear envelope; contains
• Two major classes:
- Prokaryotes nucleolus.
- Eukaryotes ➢ Nucleolus – it consists of RNA and proteins
which functions in ribosomal unit assembly.
EUKARYOTES PROKARYOTES ➢ Nucleoplasm – it surrounds the chromatin
DNA is found in the DNA is not enclosed and the nucleoli.
nucleus of the cell. within the membrane. • Function: It contains the DNA that serves as the
Contains membrane-
genetic materials for directing protein
bound organelles which Lack membrane-enclosed
synthesis.
include mitochondria, organelles.
endoplasmic reticulum,
and Golgi complex.
Cell divisions involves Usually divided by binary
mitosis. fission.

Molecular Composition of Cell

• Water accounts for about 70-75% of the weight of
the cell.
• Organic compounds accounts for 25-30% of the cell
weight.
• They are nucleic acids, proteins, polysaccharides
(carbohydrates) and lipids.
• Inorganic compounds account for the rest of the cell
weight.
 Cytoplasm Endoplasmic Reticulum
• Structure: This can be seen between the • It is further subdivided into:
plasma membrane and the nucleus where the Rough Endoplasmic Reticulum
other cellular elements are embedded. - Structure: Extensive interconnected
➢ Organelles are membrane-bound membrane network that varies in shape;
structures which carry out specific ribosomes attached on the cytoplasmic
metabolic activities of the cell. surfaces.
➢ Cytosol provides support for organelles and ➢ Ribosomes are involved in the protein
serves the viscous fluid medium. synthesis.
• Function: It is responsible for various cellular ➢ Functions: modifies, transports, and stores
processes. proteins produces by attached ribosomes.
Mitochondria
Smooth Endoplasmic Reticulum
• Structure: Double-membrane-bound - Structure: extensive interconnected
organelles containing a circular strand of DNA. membrane network lacking ribosomes.
➢ Outer Membrane is highly permeable to
small molecules, due to the presence of a
pore-forming protein called porin.
➢ Intermembrane contains many proteins
that participate in oxidative
phosphorylation.
➢ Inner membrane has multiple folds
projecting inwards, called cristae.
• Function: It is responsible for the production of
energy in the form of ATP.

Golgi Apparatus
• Structure: Series of several elongated,
flattened saclike membranous structures.
• Functions: Modifies, packages, and sorts
materials, that arrive from the endoplasmic
reticulum in transport vesicles.
➢ Vesicles transports cellular material.
Mature vesicles are called Secretory vesicles.
Lysosomes
• Structure: Spherical shaped membrane bound Peroxisomes
organelles formed from the golgi apparatus; • Structure: Smaller, spherical membrane bound
contain digestive enzymes. organelles formed the endoplasmic reticulum.
➢ The fluid inside lysosomes is much more • Functions: Detoxify specific harmful
acidic, at about pH 4.8 than the normal pH substances either produced by the cell or taken
of about 7.0-7.3 into the cell.
• Function: Digest microbes or materials by the
cell. Cytoskeleton
• Structure: Organized network of protein
filaments.
• Function: Maintains integral structural support ➢ Osmosis – is the diffusion of water point
and organization of cells. across a selectively permeable membrane.
➢ Microfilaments maintain cell shape
Cell Membrane Transport
➢ Intermediate filaments give mechanical
support to structures like nucleus and • Active Transport Process
plasma membrane. - This type of cell membrane transport uses
➢ Microtubules provides structural support. energy (ATP) provided by the cell.
- For example, cell has low intracellular
sodium; but concentration of potassium inside
the cell is very high. This is maintained by the
sodium- potassium activated ATPase,
generally called as sodium pump.

• Exocytosis refers to bulk movement of

substance out of the cell by fusions of secretory
vesicles with the plasma membrane.
• Endocytosis refers to bulk movement of
substance into the cells by vesicles forming at
the plasma membrane.

Important Notes in Prokaryotic Cell

• Prokaryotes (Eubacteria and Archaebacteria)
are the most abundant organisms on earth.
• A prokaryotic cell does not contain a membrane
bound nucleus.
• Each prokaryotic cell is surrounded by a plasma
membrane.
• The cell has no subcellular organelles, only
infoldings of the plasma membrane called
mesosomes.
Cell Life Cycle
• The deoxyribonucleic acid (DNA) is condensed • Interphase
within the cytosol to form the nucleoid. - It is the longer phase of the cell cycle where the
• Some prokaryotes have tail-like flagella. cell is active and preparing for cell division.
- The DNA molecule is duplicated exactly in a
process called DNA replication which occurs
Cell Membrane Transport
toward the end of the interphase.
• Passive Transport Process
- Diffusion is the movement of a substance from
• Cell Division
an area of its higher concentration to an area of
- Cells arise from the division of other cells.
its lower concentration.
➢ Simple Diffusion – is the type of diffusion of - Mitosis consists of four stages-prophase,
dissolved solutes through the plasma metaphase, anaphase, and telophase. The
membrane. result is two daughter nuclei, each identical to
➢ Facilitated Diffusion – is a type of diffusion the mother nucleus
that requires a protein carrier.
➢ Prophase- each chromosome consists of
two chromatids joined at the centromere.
➢ Metaphase- chromosomes align at the
center of the cell.
➢ Anaphase- chromatids separate at the
centromere and migrate to opposite poles.
➢ Telophase- two new nuclei assume their
normal structure, and cell division is
completed, producing two new daughter
cells.
 Lesson 2: CARBOHYDRATES Mass Composition Data for the Human Body
BIOCHEMISTRY - Overview
- Biochemistry - It is the study of the chemical
substances found in living organisms and the
chemical interactions of these substances with
each other
- The knowledge explosion that has occurred in
this field during the last decades of the
twentieth century and the beginning of the
twenty-first century is truly phenomenal.

BIOCHEMICAL SUBSTANCE
- It is a chemical substance found within a living
organism. OCCURRENCE AND FUNCTIONS OF
- These substances are divided into two groups: CARBOHYDRATES
o Bioinorganic substances: water and - Carbohydrates are the most abundant class of
inorganic salts bioorganic molecules on planet Earth
o Bioorganic substances: carbohydrates,
- In plants, carbohydrates constitute about 75%
lipids, proteins, and nucleic acids.
by mass of dry plant materials.
- As isolated compounds, bioinorganic and - Green (chlorophyll-containing) plants produce
bioorganic substances have no life in and of carbohydrates via photosynthesis.
themselves.
- Yet when these substances are gathered
together in a cell, their chemical interactions
are able to sustain life. - Plants have two main uses for carbohydrates
they produce:
- It is estimated that more than half of all organic
o Cellulose: serves as structural elements
carbon atoms are found in the carbohydrate
o Starch: provide energy reserves
materials of plants.
- Human uses carbohydrates of the plant - Dietary intake of plant materials is the major
kingdom extend beyond food. carbohydrate source for humans and animals.
o Carbohydrates in the form of cotton and - The average human diet should ideally about
linens are used as clothing two-thirds carbohydrates by mass.
o Carbohydrates in the form of wood are used
for shelter and heating and in making paper Functions of Carbohydrates in Humans
• Carbohydrate oxidation - provides energy
Photosynthesis • Carbohydrate storage, glycogen, provides a
- 75% of dry plant material: Produced by short-term energy source
photosynthesis • Carbohydrates supply carbon atoms for the
- Cellulose: structural element synthesis of other biochemical substances
- Starch/glycogen: energy reservoir
➢ small amount in human body
• Carbohydrates form part of the structural
framework of DNA and RNA molecules
- Plant products are source of carbohydrates
➢ average human diet contains 2/3 of • Carbohydrates linked to lipids are structural
carbohydrates. components of cell membranes
*most of the matter in plants, except water, is
carbohydrate material.
 • Carbohydrates linked to proteins function in a Polysaccharides
variety of cell-cell and cell-molecule - Contains many monosaccharide units
recognition process covalently bonded
- Polymers: May contain 100s of 1000s of
Photosynthesis monosaccharide units.
• Simpler Formula:
- CnH2On or Cn (H2O)n (hydrates of C) • Examples:
- n= number of atoms ➢ Cellulose: Paper, cotton, wood
➢ Starch: Bread, pasta, potatoes, rice, corn,
• Carbohydrates are polyhydroxy aldehydes of beans, peas, etc.
ketones or compounds that produce such
Classification of Carbohydrates
substances upon hydrolysis.
- Most simple carbohydrates have empirical
formula that fit the general formula CnH2nOn.
- Early observation by scientists that the above
mentioned formula can also be written as
Cn(H2O)n, hydrate of water.
v
- A carbohydrate is a polyhydroxy aldehyde, a
Monosaccharide polyhydroxy ketone, or a compound that yields
polyhydroxy aldehydes or polyhydroxy ketones
• Contain single polyhydroxy aldehyde or ketone
upon hydrolysis.
unit.
• They can’t be broken down into simpler
substances by hydrolysis (reaction with water)
reactions.
• Contains 3-7 atoms
• 5 and 6 carbon species are more common
• Water soluble white crystalline solids.
CHO CH2 OH
H OH O
HO H HO H Glucose and fructose
H OH H OH are monosaccharides
H OH H OH
CH2 OH CH2 OH

Glucose Fructose

Oligosaccharides
- Contains ~2-10 monosaccharide units -
covalently bonded to each other
MONOSACCHARIDE
- Disaccharides (contain 2 monosaccharide
units) more common - crystalline water soluble - Is a carbohydrate that contains a single polyhydroxy
substances aldehyde or polyhydroxy ketone unit
- Table sugar (sucrose) and milk sugar (lactose) - Cannot be broken down into simpler units by
➢ are common disaccharides hydrolysis (addition of water molecule)
- Upon hydrolysis they produce monosaccharide - Pure monosaccharides are water-soluble, white,
- In human body associated with proteins and crystalline solids.
lipids for structural and regulatory functions - Examples:
o Glucose
 o Fructose
- Two forms: left-handed and right-handed
OLIGOSACCHARIDE (mirror images)

- A carbohydrate that contains two-ten - This property in not restricted to carbohydrates

monosaccharide units covalently bonded to each
other. MIRROR IMAGE
o Disaccharide: most common type of
oligosaccharide that contains two
monosaccharide units covalently bonded to
each other.
- Example: Sucrose (table sugar)

POLYSACCCHARIDE

- A polymeric carbohydrate that contains many

monosaccharide units covalently bonded to each
other.
- Example:
o Cellulose - Is the reflection of an object in a mirror
o Starch ➢ Superimposable mirror image
• Images that coincide at all points when the
Upon hydrolysis, oligosaccharides and polysaccharides produce
monosaccharide units. image are laid upon each other
➢ Nonsuperimposable
Objects and Mirror Images • Images where not all points coincide when the
- Most monosaccharides exist in two forms: a images are laid upon each other – exists in
“left handed” and “right handed” form - same “left-handed” and “right-handed”
as two hands
- Two types of objects: - Not all molecule possesses handedness
➢ Superimposible on their mirror images: -- - Any organic molecule that contains a carbon
images that coincide at all points when the atom with 4 different groups attached to it in a
images are laid upon each other -- a dinner tetrahedral orientation possesses handedness.
plate with no design features – Achiral
➢ Non-superimposible on their mirror CHIRAL CENTER
images: Chiral (handedness) - An atom in a molecule that has 4 different
groups tetrahedrally bonded to it.
Chirality: Handedness in Molecules
- Both may be active, one may be more active or CHIRAL MOLECULE
one may be active and other non-active - a molecule whose mirror images are not
superimposable.
- Example: Right handed hormone epinephrine
is 20 times more active than left handed form
ACHIRAL MOLECULE
- a molecule whose mirror image are
- Almost all monosaccharides are right handed
superimposable.
- Amino acids are almost always left handed
- organic molecules, especially
monosaccharides, may contain more that one
HANDEDNESS
chiral center.
- An important general structure property of most
monosaccharide
- Naturally occurring monosaccharides are
almost always “right-handed”.

Stereoisomerism: Enantiomers and Diastereomers

STEREOISOMERS
- Are isomeric molecules that have the same
molecular formula and sequence of bonded atoms
but differ in three-dimensional orientation of their
atoms in space.

FEATURE THAT GENERATE STERIOISOMERISM:

- Presence of a chiral center in a molecule
- Presence of “structural rigidity” in a molecule

TWO TYPES:

1. ENANTIONAMERS
- Are stereoisomers whose molecules are
nonsuperimposable mirror images of each other
- Left- and right-handed forms of a molecule with a
single chiral center are enantiomers
- Came from the Greek word enantios, meaning Designing Handedness Using Fischer Projection
opposite Formulas
- It is two-dimension; structural notation for
2. DIASTEREOMERS showing the spatial arrangement of groups
- Are stereoisomers whose molecules are not mirror about chiral centers in molecules.
images of each other
- Examples: - Chiral center is represented as the intersection
o Cis-trans isomers of alkenes of vertical and horizontal lines.
o Cycloalkanes
- The chiral center, which is almost carbon, is not
explicitly shown.
- Molecules that contains more than on chiral center
can also exist in diastereomeric as well as
enantiomeric forms.
 AS DIASTEREOMERS
- A and C
- A and D
- B and C
- B and D
Each of these pairs are epimers – diasteromers
whose molecules differ only in the configuration at
one chiral center.

Tetrahedral Arrangements
- The four groups attached to the atom at the
chiral center assume a tetrahedral geometry
and it is governed by the following conventions
- Vertical lines from the chiral center represent
bonds to groups directed into the printed page.
- Horizontal lines from the chiral center
represent bonds to groups directed out of the
printed page

• D and L system used to designate the

handedness of glyceraldehyde enantiomers
(see figure below). In a monosaccharide
with more than one chiral carbon:
1. The carbon chain is numbered starting at
the carbonyl group of the molecule.
2. The last chiral carbon is used to determine
D or L configuration.
 ISOMERISM OPTICALLY ACTIVE COMPOUND
- A compound that rotates the plane polarized
light.
- Achiral compound – are optically inactive
- Chiral molecule – optically active

DEXOTROROTATORY COMPOUND
- Chiral compound that rotated the plane of
polarized light in a clockwise direction.

LEVOROTATORY COMPOUND
- Chiral compound that rotates the plane of
polarized light in a counterclockwise direction.
- There is no correlation between D, L and +, -
➢ In D and L you need to look at the structure
➢ + and - are determined by using a
polarimeter.
Dextrorotary and Levorotatory Compounds:
- Enantiomers are optically active: Compounds
that rotate plane polarized light

ADDITIONAL NOTATIONS
- (+) means rotation to the right (clockwise)
- (-) means rotation to the left (counterclockwise)
- D-L configuration is not directly related to + and -
designations.
- D (+) Mannose – right-handed isomer that rotates
plane- polarized light in a clockwise direction (to the
right).

Interaction between chiral compounds

- Enantiomeric pair have the same interaction
with achiral molecules and different
interactions with chiral molecules.
Properties of Enantiomers
1. Enantiomers have indentical:
- When plane-polarized light is passed through a
- Boiling points
solution containing a single enantiomer, the
- Melting points
plane of the polarized light is rotated
- Densities
counterclockwise (to the left) or clockwise (to
- Intermolecular force strength
the right), depending on the enantiomer.
2. A pair of enantiomers have the same
- The extent of rotation depends on the solubility in a achiral solvent, such as
concentration of the enantiomers as well on its ethanol, but differing solubilities in a chiral
identity solvent, such as ethanol, but differing
- The two enantiomers of a pair rotate the plane- solubilities in a chiral solvent, such as D-2
polarized light the same number of degrees, but Butanol.
in opposite directions.
3. The rate and extent of reaction of
- Enantiomers are sometimes called optical
enantiomers with another reactant are the
isomers.
 same if the reactant is achiral but differ if
the reactant is chiral.
4. Receptor sites for molecule within the body
have chirality associated with them.
Examples:
- Spearmint (D-Carvone) and Caraway (L-
Carvone)
- D- Epinephrine (perfect fit with the cellular
receptor) and L-Epinephrine.

• Our body responds differently to different

enantiomers:
• One may give higher rate or one may be
inactive
– Example: Body response to D form
of hormone epinephrine is 20 times
greater than its L isomer

Classification of Monosaccharide
- The term saccharide comes from the Latin word
for “sugar”, which is saccharum.
Triose --- 3 carbon atoms
Tetrose -- 4 carbon atoms
Pentoses – 5 carbon atoms
Hexoses -- 6 carbon atoms
Aldoses: Monosaccharides with one aldehyde group
Ketoses: Monosaccharides with one ketone group
• Combined # of C atoms and functional group:
- Example: Aldohexose: Monosaccharide with
aldehyde group and 6 C atoms
Aldose
- A monosaccharide that contains an aldehyde
functional group.
- A polyhydroxy aldehyde
Ketose
- A monosaccharide that contains a ketone
functional group.
- A polyhydroxy ketone
 Biochemically Important Monosaccharide - Also called” brain sugar” because it is a
1. Most abundant in nature component of glycoproteins (protein-
2. Nutritionally most important carbohydrate compounds) found in brain and
3. Grape fruit good source of nerve tissue.
glucose (20-30% by mass) – also - Also present in the chemical markers that
named grape sugar, dextrose and distinguish various types of blood – A, B, AB, and O
blood sugar (70-100 mg/mL of
blood) D-FRUCTOSE
4. Six membered cyclic form - Most important ketohexose
- Also known as levulose and fruit sugar
- The sweetest- tasting of all sugars
1. Ketohexose - Found in fruits and honey
2. Sweetest tasting of all sugars - Sometimes used as dietary sugar
3. Found in many fruits and in - Different in C-1 and C-2 with D-glucose
honey
4. Good dietary sugar – due to D- RIBOSE
higher sweetness - An aldopentose
5. Five membered cyclic form - A component of a variety of complex molecules
such as RNA and ATP.
- The compound 2-Deoxy D-ribose is an
D-GLYCERALDEHYDE AND DIHYDROXYACETONE important component in nucleic acid
- The simplest of the monosaccharides chemistry.
- Are important intermediates in the process of
glycolysis.

D-GLUCOSE
- Ripe fruits are a good source of glucose, which Cyclic Forms of Monosaccharides
is often referred to as grape sugar. - Experimental evidence indicates that for
- Often names are dextrose and blood sugar. monosaccharides containing five or more
- The normal glucose in human blood is in the carbon atoms, such open-chain structures are
range of 70-100 mg/dL (1 dL= 100mL) actually in equilibrium which two cyclic
- Cells use glucose as a primary source of energy. structures, and the cyclic structures are the
predominant forms at equilibrium.
D-GALACTOSE
- D-Galactose and D-Glucose are epimers (C-4)
- Seldom encountered as a free monosaccharide
- In the human body, it is synthesized from
glucose in the mammary glands for use in
lactose (milk sugar), a disaccharide consisting
of a glucose unit and galactose unit.
RECALL:
- Hemiacetals – both -OH and -OR groups are
attached to the same carbon atom

PYRANOSE – a cyclic monosaccharide that

contains a six-atom ring.

FURANOSE – a cyclic monosaccharide that

- Monosaccharides – the -OH and -OR groups contains a five-atom ring,
are attached to the carbonyl carbon.
- The cyclic forms of monosaccharides result
from the ability of their carbonyl group.
- Cyclization of glucose (hemiacetal) creates a
new chiral center at carbon 1, and the presence
of this new chiral center produce two
stereoisomers, called α and β isomers.

HANWORTH PROJECTION FORMULA

- A Haworth projection formula is a two-
dimensional structural notation that specifies
the three-dimensional structure of a cyclic form
of a monosaccharide.
- In an aqueous solution of D-Glucose, a dynamic - It is a two-dimensional structural notation that
equilibrium exists among the α, β and open- specifies the three-dimensional structure of a
chain forms, and there is continual cyclic form of a monosaccharide.
interconversion among them. - It is from Walter Norman Hanworth
 CH2 OH - Other aldoses, as well as ketoses, undergo
similar reactions.
O

OXIDATION
OH
• Oxidation to acidic sugars: The redox
OH OH chemistry of monosaccharides is closely
linked to the alcohol and aldehyde functional
OH
groups present in them.
-D-Glucose • Oxidation can yield three different types of
CH2OH
CH2OH
O
CH2OH
O acidic sugars depending on the type of oxidizing
OH agent used:
OH
➢ Weak oxidizing agents
OH
OH OH OH - Tollens and Benedict’s solutions/reagents
 -D-Fructose  -D-Ribose oxidize the aldehyde end to give an aldonic acid.
Hanworth Projection Formula: - Aldoses are converted into aldonic acid
ALPHA AND BETA CONFIGURATION ➢ Aldoses are reducing sugars o Reduces Ag+
- Alpha or Beta configuration is determined by to Ag in Tollen’s Reagent o Reduces Cu2+ to
the position of the —OH group on C1 relative to Cu+ in Benedict’s Reagent
the CH2OH group that determines D or L series. ➢ A reducing sugar is a carbohydrate that
gives a positive test with Tollens and
- In a Beta configuration, both of these groups
Benedict’s solutions.
point in the same direction
- In an Alpha configuration, the two groups point ➢ Strong Oxidizing Agents
in opposite directions. - Strong oxidizing agents can oxidize both ends
of a monosaccharide at the same time (the
Hanworth Projection Formula: carbonyl group and the terminal primary
OH GROUP alcohol group) to produce a dicarboxylic acid:
- The specific identity of a monosaccharide is ➢ Such polyhydroxy dicarboxylic acids are
determined by the positioning of the other known as aldaric acids.
—OH groups in the Haworth projection Oxidization
formula. - In biochemical systems enzymes can oxidize
- Any —OH group at a chiral center that is to the the primary alcohol end of an aldose such as
right in a Fischer projection formula points glucose, without oxidation of the aldehyde
down in the Haworth projection formula and group, to produce an alduronic acid.
any —OH group to the left in a Fischer
projection formula points up in the Haworth Sugar Alcohols
projection formula. • Reduction to sugar alcohols: The carbonyl
group in a monosaccharide (either an aldose
Reactions of Monosaccharides or a ketose) is reduced to a hydroxyl group
1. Oxidation to acidic sugars using hydrogen as the reducing agent.
2. Reduction to sugar alcohols ➢ The product is the corresponding
3. Glycoside formation polyhydroxy alcohol - sugar alcohol.
4. Phosphate ester formation ➢ Sorbitol - used as moisturizing agents in
5. Amino acid sugar formation foods and cosmetics and as a sweetening
agent in chewing gum.
- These reactions will be considered with D-GLUCITOL - - Common name is D-Sorbitol that is used
respect to glucose. as moisturizer in foods and cosmetics Used as
sweetening agent in chewing gum because it cannot be - Phosphate esters of various monosaccharides
used by bacteria as their food are stable in aqueous solution and play
important roles in the metabolism of
Glycoside carbohydrates.
• Glycoside formation: Cyclic forms of
monosaccharides are hemiacetals, they Amino Sugar Formation
react with alcohols to form acetals: - An amino sugar - one of the hydroxyl groups of a
- Monosaccharide acetals are called glycoside monosaccharide is replaced with an amino
group
• A GLYCOSIDE is an acetal formed from a cyclic
monosaccharide by replacement of the - In naturally occurring amino sugars the carbon
hemiacetal carbon —OH group with an —OR 2 hydroxyl group is replaced by an amino group
group:
➢ A glycoside produced from glucose – - Amino sugars and their N-acetyl derivatives are
glucoside important building blocks of polysaccharides
➢ A glycoside produced from galactose – such as chitin
galactoside
Disaccharides
➢ Glycosides exist in both Alpha and Beta
- Two monosaccharides can react to form
forms
disaccharide
- One monosaccharide act as a hemiacetal and
Blood Types and Monosaccharides other as alcohol
• Blood Types and Monosaccharides: Human
blood is classified into four types: A, B, AB, CELLOBOISE
and O: • Cellobiose is produced as an intermediate in
➢ Blood of one type cannot be given to a the hydrolysis of the polysaccharide
recipient with blood of another type. cellulose:
➢ A transfusion of wrong blood type can cause ➢ Cellobiose contains two b - D-glucose
the blood cells to form clumps - a monosaccharide units linked through a b
potentially fatal reaction. (1—4) glycosidic linkage.
➢ People with type O blood are universal CH2OH
donors, and those with type AB blood are
O OH
universal recipients. CH2OH  (1-4)
H
O OH
BLOOD TYPES: O
- In the United States type O blood is the most OH
common and type A the second most OH
common. OH
- The biochemical basis for the various blood OH
types involves monosaccharides present on Cellobiose
plasma membranes of red blood cells.
- The monosaccharides responsible for blood
groups are D-galactose and its derivatives. GLYCOSIDIC LINKAGE
- Is the bond in a disaccharide resulting from the
Phosphate Ester Formation reaction between the hemiacetal carbon atom –OH
- The hydroxyl groups of a monosaccharide can group of one monosaccharide and an –OH group on
react with inorganic oxyacids to form inorganic the other monosaccharide.
esters.
- Always carbon-oxygen-carbon bond
MALTOSE • Sucrose (table sugar): The most abundant of
- Often called malt sugar all disaccharides and found in plants.
- Comes from the breakdown of starch • It is produced commercially from the juice of
- Common ingredient in baby foods and in malted sugar cane and sugar beets.
sugar • Sugar cane contains up to 20% by mass sucrose
- Made up of 2 D-Glucose units • Sugar beets contain up to 17% by mass sucrose
- A reducing sugar
- The most important chemical reaction of maltose is CH2 OH
that of hydrolysis producing 2 D-Glucose units O
- Acidic condition is needed or maltase is needed CH2 OH
OH
O
OH OH

OH OH

-D-Glucose
LACTOSE
OH

 (1-2)
• Lactose is made up of b-D-galactose unit and a + OH
O
Linkage
CH2 OH CH2 OH
b-D-glucose unit joined by a b(1-4) glycosidic O OH O

linkage OH OH

CH 2OH CH 2OH

• Lactose - principal carbohydrate in milk. OH OH

• Human - 7%–8% lactose -D-Fructose Sucrose

• cow’s milk - 4%–5% lactose
• Lactose intolerance: a condition in which General Characteristics of Polysaccharides
people lack the enzyme lactase needed to THE POLYMER CHAIN
hydrolyze lactose to galactose and glucose. - Polymers
• Lactase hydrolyzes b(1-4) glycosidic linkages. - Many monosaccharide units bonded with
• Deficiency of lactase can be caused by a glycosidic linkages
genetic defect, physiological decline with age, - Two Types:
or by injuries to intestinal mucosa. ➢ Linear and Branched, homo- and hetero-
polysaccharides.
• When lactose is undigested it attracts water
causing fullness, discomfort, cramping,
nausea, and diarrhea. Bacterial fermentation of
the lactose further along the intestinal tract
produces acid (lactic acid) and gas, adding to
the discomfort
CH2OH
O OH
 (1-4)
CH2OH H
OH
OH O O
OH
OH

OH
Lactose
SUCROSE
STORAGE POLYSACCHARIDE - Molecular Mass: 3,000,000 (up to 1,000,000
• Polysaccharides are not sweet and don’t show glucose units)
positive tests with Tollen’s and Benedict’s - Three times more highly branched than
solutions whereas monosaccharides are sweet amylopectin in starch
and show positive tests - Excess glucose in blood stored in the form of
• Limited water solubility glycogen
• Examples: - Sometimes referred to as animal starch
– Cellulose, starch in plants - Liver cells and muscle cells are the storage sites
– Glycogen in animals for glycogen in humans
– Chitin in arthropods - Muscle tissue – approximately 1% glycogen
- Liver tissue – 2-3% glycogen
STARCH
- This amount is enough to take care the
• A storage polysaccharide is a polysaccharide
demands of the body for 15 hours
that is a storage form for monosaccharides
and is used as an energy source in cells. - During strenuous activities, glycogen supplies
Starch: can be exhausted rapidly thus the body begins
- Glucose is the monomeric unit to oxidize fat as a source of energy
- Storage polysaccharide in plants - Athletes do “carbohydrate loading”
- Two types of polysaccharides isolated from - When excess glucose is present in the blood,
starch: the liver and the muscle tissue convert the
➢ Amylose: Straight chain polymer - 15 - 20% excess glucose to glycogen for storage
of the starch and has a (1 → 4) glycosidic - Whenever the glucose blood level drops, some
bonds stored glycogen is hydrolyzed back to glucose
➢ Molecular Mass: 50,000 (up to 1000 - Formation of glycogen reduces osmotic
glucose units) pressure within the cells and prevents it from
living the cells
AMYLOPECTIN STRUCTURE
• Amylopectin:
– Branched chain polymer - 80 - 85 % of the
starch a (1→4) glycosidic bond for straight
chain and a (1→6) for branch
– Molecular Mass: 300,000 (up to 100,000 STRUCTURAL POLYSACCHARIDES
glucose units) - higher than amylose. CELLULOSE
– Human can hydrolyze alpha linkage but not - Linear homopolysaccharide with b (1 → 4)
beta linkage. glycosidic bond.
– Iodine is often used for the presence of starch
in solution. - Up to 5000 glucose units with molecular mass
– Starch-containing solutions turn a dark blue- of 900,000 amu.
black when iodine is added
– As starch is broken down through acid or - Cotton ~95% cellulose and wood ~50%
enzymatic hydrolysis to glucose monomers, cellulose.
the blue-black color disappears.
- Humans don’t have enzymes that hydrolyze b (1
GLYCOGEN → 4) - so humans can not digest cellulose --
- Humans and animals’ storage polysaccharide animals also lack these enzymes but they can
- Contains only glucose units digest cellulose because they have bacteria in
- Branched chain polymer – a (1→4) glycosidic their guts to hydrolyze cellulose
bonds in straight chains and a (1→6) in
branches
- It serves as dietary fiber in food-- readily HYALURONIC ACID
absorbs water and results in softer stools - Alternating residues of N-acetyl-b-D-glucosamine
- 20 - 35 g of dietary fiber is desired everyday and D-glucuronic acid.
HO

HO O O - Highly viscous - serve as lubricants in the fluid of

HO O O
OH
joints and part vitreous humor of the eye.
OH (1-4) OH
HO O O
OH (1-4)
O O OH
OH (1-4)
O OH
OH

CHITIN
- Similar to cellulose in both function and
structure. HEPARIN
- An anticoagulant-prevents blood clot.
- Linear polymer with all b (1→4) glycosidic - Polysaccharide with 15–90 disaccharide
linkages - it has a N-acetyl amino derivative of residues per chain.
glucose

- Function is to give rigidity to the exoskeleton s of

crabs, lobsters, shrimp, insects, and other
arthropods.

GLYCOLIPIDS AND GLYCOPROTEINS: CELL

RECOGNITION
• A glycolipid is a lipid molecule that has one or
more carbohydrate (or carbohydrate derivative)
Acidic Polysaccharides units covalently bonded to it.
• Acidic polysaccharides - polysaccharides with • A glycoprotein is a protein molecule that has
a repeating disaccharide unit containing an one or more carbohydrate (or carbohydrate
amino sugar and a sugar with a negative charge derivative) units covalently bonded to it.
due to a sulfate or a carboxyl group.
• Structural polysaccharide present in
• The lipid or protein part of the glycolipids is
connective tissue associated with joints,
incorporated into the cell membrane structure
cartilage, synovial fluids in animals and humans
and the carbohydrate (oligosaccharide) part
– Primary function is lubrication
functions as a marker on the outer cell
necessary for joint movement
membrane surface
– These are heteropolysaccharides -
have more than one type of
• In the human reproductive process, fertilization
monosaccharide monomers is
involves binding interaction between
present.
oligosaccharide markers on the outer
➢ Examples:
membrane surface of an ovulated egg and
– Hyaluronic acid
protein receptor sites on a sperm cell
– Heparin
membrane.
 DIETARY CONSIDERATIONS AND
CARBOHYDRATES
NUTRITION
• Foods high in carbs content constitute over
50% of the diet of most people of the world --
a balanced dietary food should contain about
60% of carbohydrate:
– Corn in South America
– Rice in Asia
– Starchy root vegetables in parts of Africa
– Potato and wheat in North America

• Nutritionist divide dietary carbs into two

classes:
– Simple carb: dietary monosaccharides or
disaccharides - sweet to taste commonly
referred to as sugars - 20 % of the energy in
the US die
– Complex carbs: Dietary polysaccharides --
starch and cellulose - normally not sweet to
taste.

GLYCEMIC FOODS
• A developing concern about intake of
carbohydrates involves how fast the given
dietary carbs are broken down to glucose within
the human body

• Glycemic effect refers to:

– how quickly carbs are digested
– how high blood glucose rise
– how quickly blood glucose levels return
to normal
• Glycemic index (GI) has been developed for
rating foods
 Lesson 3: LIPIDS
STRUCTURE AND CLASSIFICATIONS OF LIPIDS
LIPID
- is an organic compound found in living
organisms that is insoluble (or only sparingly
soluble) in water but soluble in non-polar
organic solvents.
- Unlike other biomolecules, lipids do not have a
common structural feature that serves as the
basis for defining such compounds.
- They are classified on the basis of solubility not
on any functional groups:
➢ Insoluble or sparingly soluble in water
➢ Soluble in non-polar organic solvents

Five Categories of Lipids

For purposes of simplicity of study lipids are divided TYPES OF FATTY ACIDS
into five categories based on their function: SATURATED AND UNSATURATED FATTY ACIDS
1. Energy-Storage Lipids - Carboxylic acids with linear (unbranched) carbon
- Triacylglycerols chain - Fatty acids are naturally occurring
monocarboxylic acids
2. Membrane Lipids
- Phospholipids - Even number of Carbon atoms:
- Sphingoglycolipids ➢ Long chain fatty acids: C12 - C26
- Cholesterol ➢ Medium chain fatty acids: C6 – C11
3. Emulsification Lipids ➢ Short-chain fatty acids: C4 – C5
- Bile acids
Two types:
4. Chemical Messenger Lipids
- Steroid hormones ➢ Saturated - all C-C bonds are single bonds
- Eicosanoids ➢ Unsaturated o Monounsaturated: one C=C
5. Protective-coating Lipids bond
- Biological waxes ➢ Polyunsaturated: 2 or more C=C bonds
present - up to six double bonds are present in
Structural Formulas fatty acids
- Lipids exhibit structural diversity
Saturated Fatty Acids
- Some are esters, some are amides, and some
are alcohols (acyclic and cyclic) and some are - Numbering starts from the end of -COOH group
- See structural notation: it indicates number of C
polycyclic.
atoms
➢ Lauric acid has 12 C atoms and no double
bonds so it is (12:0)
 Unsaturated Fatty Acids
- A monounsaturated fatty acid is a fatty acid - Linoleic Acid Deficiency:
with a carbon chain in which one carbon– ➢ Skin redness - becomes irritated
carbon double bond is present. ➢ Infections and dehydration
- Different ways of depicting the structure ➢ Liver abnormalities
➢ Children need it the most
➢ Human milk has more than cow’s milk

AMERICAN DIET
- Sufficient in omega 6 fatty acids
- Deficient in omega 3 fatty acids
➢ Fish: good source for omega 3 fatty acids
- High rate of heart disease may be due to
imbalance in omega 3 and 6 fatty acids
➢ Ideal ratio – Omega 6 : Omega 3 (4-10 g: 1g)
PHYSICAL PROPERTIES OF FATTY ACIDS

PHYSICAL PROPERTIES OF FATTY ACIDS

Polyunsaturated Fatty Acids (PUFAs) WATER SOLUBILITY
- A polyunsaturated fatty acid is a fatty acid with - Short chain fatty acids have some solubility
a carbon chain in which two or more carbon– whereas long chain fatty acids are insoluble.
carbon double bonds are present. - Short chain fatty acids are sparingly soluble
- Up to six double bonds are found in because of carboxylic acid polar group.
biochemically important PUFAs. - Physical properties such as melting point
depends on the number of C atoms and degree
- Two types of unsaturated fatty acids: unsaturation.
➢ Omega (ω)-3 fatty acids: An unsaturated
fatty acid with its endmost double bond THE MELTING POINT
three carbon atoms away from its methyl The melting point depends upon:
end. - Length of carbon chain
➢ Omega(ω)-6 fatty acid: is an unsaturated - Degree of unsaturation (number of double
fatty acid with its endmost double bond six bonds in a molecule)
carbon atoms away from its methyl end.

Selected Unsaturated Fatty Acids of Biological

Importance
- Numbering starts from the other end of COOH
- See structural notation: it indicates number of C
atoms
➢ 18:2 - 18 carbons, 2 double bonds
Omega Acids
ESSENTIAL FATTY ACIDS
- Must be part of diet
- Nutritionally important Omega-3 and Omega-6
fatty acids
➢ Linolenic acid – Omega-3 SPACE-FILING MOLECULES
➢ Linoleic acid – Omega-6
- The number of bends in a fatty acid chain DIFFERENCE OF FATS AND OILS
increase as the number of double bonds PHYSICAL STATE
increase Fats Oils
➢ Less packing occurs Predominantly Saturated Predominantly Unsaturated
Solids or semisolids at room Liquids at room temperature
➢ Melting point is lower
temperature
➢ Tend to be liquids at room temperature Source
Fats Oil
Animal source and tasteless Plants and fish oil
Pure oils and fats are colorless, ordorless

DIETARY CONSIDERATIONS AND

TRIACYLGLYCEROLS
“GOOD FATS” versus “BAD FATS”
- Studies indicate that type of dietary fat and amount
of dietary fat are important for balanced diet:
Current recommended
Total fat intake in calories
amounts are
15% Monounsaturated fat
10% Polyunsaturated
< 10% Saturated fats
Good Fats Bad Fats
ENERGY-STORAGE LIPIDS: TRIACYLGYCEROLS Monounsaturated Fats Saturated Fat
ENERGY-STORAGE MATERIALS Omega 3 and 6 Trans-monounsaturated fats
- With the Notable exception of nerve cells, Polyunsaturated fats

human cells store small amounts of energy Essential Fatty Acids

providing materials: - Fatty acids that must be obtained from dietary
➢ The most widespread energy storage sources – are not synthesized within the body
material – carbohydrate glycogen - Two most important essential fatty acids are:
➢ Present in small amounts ➢ Linoleic acid (18:2) - omega 6
➢ Linolenic acid (18:3) - omega 3 Both are
- Storage material is the triacylglycerols needed for:
➢ Triacylglycerols are concentrated primarily ▪ Proper membrane structure
in special cell (adipocytes) ▪ Serve as starting materials for the
➢ Nearly filled with the material production of several nutritionally
important longer-chain omega-6 and
TWO TYPES OF TRIACYLGLYCEROLS omega-3 fatty acids
a. Simple Triacylglycerols - Deficiencies of above two acids may result in
- Three identical fatty acids are esterified skin redness, infections and dehydration likely
- Naturally occurring simple triacylglycerols
and liver abnormalities may develop.
b. Mixed Triacylglycerols FAT AND FATTY ACID COMPOSITION OF NUTS -
- A triester formed from the esterification of Numerous studies now indicate that eating nuts
glycerol with more than one kind of fatty acid. can have a strong protective effect against coronary
- In nature mostly mixed triacylglycerols are heart disease:
found and are different even from the same ➢ Low amounts of saturated fatty acids
source depending on the feed ➢ Nuts also contain valuable antioxidant
➢ Corn vitamins, minerals, and plant fiber protein
➢ Peanut
➢ Wheat – fed cows have different
triacylglycerols
 CHEMICAL REACTIONS OF TRIACYLGLYCEROLS Membrane Lipids: PHOSPHOLIPIDS
PARTIAL HYDROLYSIS - All cells are surrounded by a membrane that
- Chemical properties due to two functional confines their contents.
groups: ester and alkenes - Up to 80% of the mass of a cell membrane can
➢ Hydrolysis: Partial hydrolysis of be lipid materials and these lipid materials are
triacylglycerols. dominated by phospholipids.
➢ Breaking of 1-2 ester bonds to give rise to
mono- or diacylglycerol and fatty acid(s)
➢ Carried out by enzymes produced by the PHOSPHOLIPIDS
pancreas - A phospholipid contains one or more fatty
acids, a phosphate group, a platform molecule
(glycerol or sphingosine) to which the fatty
SPONIFICATION acid(s) and the phosphate group are attached,
- Hydrolysis in basic solution: Produce salt of and an alcohol that is attached to the
fatty acid and glycerol phosphate group.
RCOOR’ + NaOH → RCOONa (soap) + R’OH
O
H 2 C OH
GLYCEROPHOSPHOLIPIDS
H 2C O C R
O - A glycerophospholipid is a lipid that contains
HC OH + 3RCOONa
R C O CH
O
+ 3NaOH
two fatty acids and a phosphate group
Soap
H 2C O C R H 2 C OH
esterified to a glycerol molecule and an
alcohol esterified to the phosphate group.
HYDROGENATION - All attachments (bonds) between groups in a
- Addition of hydrogen across double (=) bond - glycerophospholipid are ester linkages
increases degree of saturation. - Glycerophospholipids have four ester linkages
O
H2C O C
O
H2C O C
as contrasted to three ester linkages in
HC O C
O
+ 2H2
O triacylglycerols.
- Glycerophospholipids undergo hydrolysis
HC O C
O O
H2C O C
H2C O C and saponification reactions in a manner
Oil Solid similar to that for triacylglycerols
- Many food products are produced by partial - The alcohol attached to the phosphate group in
hydrogenation of oils and fats a glycophospholipid is usually one of three
- Peanut oil + H2 → Peanut Butter amino alcohols:
- Vegetable oil + H2 → Margerine ➢ Choline/Phosphatidylcholines
➢ Ethanolamine / Phosphatidylethanolamines
OXIDATION ➢ Serine - respectively known as
- Double bonds in triacylglycerols are subject phosphatidylcholines,
to oxidation with oxygen in air (an oxidizing phosphatidylethanolamines, and
agent )-Leads to C=C breakage. phosphatidylserines.
- Remember that oxidation of alkenes may result
into two short chain molecules – an aldehydes - Structurally glycerophospholipids are
or a carboxylic acid: although similar to triacylglycerols, they have
➢ The aldehydes and/or carboxylic acids so different biochemical functions.
produced often have objectionable odors - ➢ Triacylglycerols serve as energy storage
fats and oils are said to be rancid molecules
➢ To avoid this unwanted oxidation process ➢ Glycerophospholipids function as
antioxidants are added as preservatives, components of cell membranes
e.g., Vitamin C and vitamin E are good - A major structural difference between the two
antioxidant preservatives. types of lipids is that of their “polarity” –
 Responsible for the their differing biochemical GANGLIOSIDES
functions. - Complex sphingoglycolipids are called
➢ Triacylglycerols are a non-polar Gangliosides:
➢ Glycerophospholipids are polar. ➢ contain a branched chain of up to seven
monosaccharide residues.
- Occur in the gray matter of the brain as well as in the
myelin sheath.
SPHINOGOPHOSPHOLIPIDS
Membrane Lipids: CHOLESTEROL
- Structures based on the 18-carbon
monounsaturated aminodialcohol CHOLESTEROL: THIRD MAJOR TYPE OF
sphingosine MEMBRANE LIPID
- contains one fatty acid and one phosphate - Lipids: Fused Rings
group attached to a sphingosine molecule and - Cholesterol: C27 steroid molecule
an alcohol attached to the phosphate group - A steroid is a lipid whose structure is based
- Saponifiable lipids on a fused ring system of three 6 carbon rings
- Sphingophospholipids in which the alcohol and one 5 carbon ring.
esterified to the phosphate group is choline are - Important in human cell membranes, nerve
called sphingomyelins. tissue and brain tissue
- Sphingomyelins are found in all cell ➢ Important in chemical synthesis:
membranes and are important structural Hormones, vitamins essential for life
components of the myelin sheath of neurons
Cholesterol in Food:
Membrane Lipids: Sphingoglycolipids - Liver synthesizes cholesterol: ~ 1g everyday;
SPHINGOGLYCOLIPIDS so it is not necessary to consume in the form
- Contains both a fatty acid and carbohydrate of diet.
- Cholesterol synthesis decrease if it is
SIMPLE SPHINGOGLYCOLIPIDS ingested but reduction is not sufficient:
- Are called cerebrosides Leads to cardiovascular disease
- Contains a single monosaccharide unit – either ➢ Animal Food: Lot of cholesterol
glucose or galactose ➢ Plant Food: No cholesterol
➢ They occur primarily in brain (7% of dry mass)
Cell Membrane
CELLS
- Cells are surrounded by plasma membranes:
➢ Separates aqueous interior of a cell from the
aqueous environment surrounding the cell.
➢ Up to 80% of plasma membrane is lipid
material.
➢ The membranes are lipid bilayer made up of
phospholipids.
- Cells are surrounded by plasma membranes:
➢ Bilayer: Nonpolar tails of phospholipids in the
middle and polar heads are on the surface
▪ 6 - 9 billionths of a meter thick or 6-9
nanometer thick
➢ The membrane is a liquid like structure due to
unsaturation in lipid tails
CHOLESTEROL PASSIVE TRANSPORT
- Cholesterol molecules are also components of - Transport Across Cell Membranes:
plasma membranes: ➢ To maintain cellular processes various
➢ Cholesterol helps regulate membrane fluidity molecules transported across the cell
– The fused ring system does nor allow rotation membranes.
of fatty acid tails in the vicinity
Three types of transport.
➢ Fits between fatty acid chains of the lipid
bilayer: Make it rigid - Passive transport
➢ Cholesterol thus acts a membrane plasticizer - Facilitated transport
- Active transport
Passive transport - a substance moves across a cell
membrane by diffusion from a region of higher
concentration to a region of lower concentration.
- Only a few types of molecules, including O2, N2,
H2O, urea, and ethanol, can cross membranes by
passive transport
Facilitated transport - a substance moves across a
PROTEINS
cell membrane with the aid of a membrane protein
- The membranes also contain proteins: from a region of higher concentration to a region of
➢ Responsible for moving substances such as lower concentration.
nutrients and electrolytes across the
- The specific protein carriers or transporters are
membrane
involved in the process.
➢ Receptors for hormones and
neurotransmitters Active transport - a substance moves across a cell
membrane, with the aid of membrane proteins,
- The membrane proteins and some lipids are
against a concentration gradient with the expenditure
further reacted with carbohydrates molecules:
of cellular energy.
➢ Act as markers: process by which different
cells recognize each other. - Proteins involved in active transport are called
“pumps.” The needed energy is supplied by
molecules such as ATP.
EMULSIFICATION LIPIDS: BILE ACIDS
- An emulsifier is a substance that can disperse
and stabilize water-insoluble substances as
colloidal particles in an aqueous solution.
- Bile Acids: Cholesterol derivatives that
functions as emulsifying agents that make
dietary lipids soluble in aqueous environment
of the digestive tract:
➢ Approximately one third of cholesterol
produced by liver is converted to bile acids.
➢ Action similar to soap in washing
BILE ACIDS ADRENOCOTICOID HORMONES
- Bile acids are tri- or dihydroxy cholesterol - Produced by the adrenal glands - small organs
derivatives. located on top of each kidney
- The carbon 17 side chain of cholesterol has - 28 Different hormones have been isolated from
been oxidized to a carboxylic acid. the adrenal cortex
- The oxidized acid side chain is bonded to an - Two types of adrenocorticoid hormones:
amino acid (either glycine or taurine) through ➢ Mineralocorticoids - control the balance of
an amide linkage. Na and K ions in cells
- Bile is a fluid containing emulsifying agents ➢ Glucocorticoids - control glucose
(Bile acids) secreted by the liver, stored in the metabolism and counteract inflammation
gallbladder, and released into the small
intestine during digestion. MESSENGER LIPIDS: EICOSANOIDS
• Eicosanoids Arachidonic acid (20:4)
MESSENGER LIPIDS: STEROID HORMONES derivatives:
HORMONES ➢ Have profound physiological effects at
- A hormone is a biochemical substance extremely low concentrations.
produced by a ductless gland that has a ➢ Eicosanoids are hormone-like molecules
messenger function. ➢ Exert their effects in the tissues where they
- Hormones serve as a means of communication are synthesized.
between various tissues. ➢ Eicosanoids usually have a very short “life.”
➢ Some hormones are lipids.
➢ Physiological effects of eicosanoids:
- The lipids that play the role of “chemical • Inflammatory response
messengers” include: • Production of pain and fever
➢ Steroid hormones – derivatives of • Regulation of blood pressure
cholesterol • Induction of blood clotting
➢ Eicosanoids- derivatives of arachidonic • Control of reproductive functions, such as
acid induction of labor
- There are two major classes of steroid • Regulation of the sleep/wake cycle
hormones:
➢ Sex hormones - control reproduction and THREE PRINCIPLES TYPES
secondary sex characteristics 1. Prostoglandins: C20-fatty-acid derivative
➢ Adrenocorticoid hormones – control containing cyclopentane ring and oxygen-
numerous biochemical processes in the containing functional groups
body. – Involved in raising body temperature,
– Inhibiting the secretion of gastric juices,
Sex Hormones – Increasing the secretion of a protective
- Classified into three major groups: mucus layer into the stomach,
➢ Estrogens - the female sex hormones – Relaxing and contracting smooth muscle,
➢ Androgens - the male sex hormones directing water and electrolyte balance,
➢ Progestins - the pregnancy hormones intensifying pain, and enhancing
inflammation responses.

2. Thromboxanes: C20-fatty-acid derivative

containing a cyclic ether ring and oxygen-
containing functional groups
• Promote platelet aggregation.
3. Leukotrienes: C20-fatty-acid derivative
containing three conjugated double bonds and
hydroxy groups
• Promote inflammatory and hypersensitivity
(allergy) responses

PROTECTIVE-COATING LIPIDS:
- A biological wax: a monoester of a long-chain
fatty acid and a long-chain alcohol.
- The fatty acids found in biological waxes:
➢ Generally are saturated fatty acids
➢ Contain 14 to 36 carbon atoms.

- The alcohols found in biological waxes:

➢ May be saturated or unsaturated
➢ May contain 16 to 30 carbon atoms.

• Properties of Biological waxes : Water-

insoluble and water-repellent because of long
nonpolar hydrocarbon chains.
➢ Humans and animals secrete biological
waxes from skin glands
• Function of biological waxes:
➢ Protect hair and skin; and keep it pliable and
lubricated.
➢ Impart water repellency to animal fur.
➢ Birds keep their feathers water repellent
and help minimize loss of body heat
➢ Plants coat their leaves with a thin layer of
biological waxes to prevent excessive
evaporation of water and to protect against
parasite attack.
 Lesson 4: CHARACTERISTICS OF PROTEIN - Non-polar amino acids: R-groups are non-
PROTEIN/S polar.
- A protein is a naturally-occurring, unbranched ➢ Such amino acids are hydrophobic-water
polymer in which the monomer units are amino fearing (insoluble in water).
acids. ➢ 8 of the 20 standard amino acids are non-
- Proteins are most abundant molecules in the polar.
cells after water- account for about 15% of a ➢ When present in proteins, they are located
cell’s overall mass. in the interior of protein where there is no
- Elemental Composition – Contain Carbon (C), polarity.
Hydrogen (H), Nitrogen (N), Oxygen (O), most
also contain Sulfur (S). - Polar Amino Acids: R-groups are polar
- The average nitrogen content of proteins is ➢ Three types: Polar neutral; Polar acidic;
15.4% by mass. Polar basic.
- Also present are Iron (Fe), Phosphorus (P), and → Polar-neutral: contains polar but neutral side
some metals in some specialized proteins. chains
➢ Seven amino acids belong to this category.
AMINO ACIDS: The Building Blocks for Protein → Polar acidic: Contain carboxyl group as part of
Amino Acid the side chains.
- An organic compound that contains both an ➢ Two amino acids belong to this category.
amino (-NH2) and carboxyl (-COOH) groups → Polar basic: contain amino group as part of
attached to same carbon atom. the side chain.
➢ The position of carbon atom is Alpha (a) ➢ Two amino acids belong to this category.
➢ -NH2 group is attached at alpha (a) carbon
atom.
NOMENCLATURE
➢ -COOH group is attached at alpha (a)
- Common names assigned to the amino acids
carbon atom.
are currently used.
- Three letter abbreviations - widely used for
- R= side chain – vary in size, shape, charge,
naming:
acidity, functional groups present, hydrogen-
➢ First letter of amino acid name is
bonding ability, and chemical reactivity.
compulsory and capitalized followed by
➢ > 700 amino acids are known
next two letters not capitalized except in the
➢ Based on common “R” groups, there are 20
case of Asparagine (Asn), Glutamine (Gln)
standard amino acids.
and tryptophan (Trp).
Side Chain
- One-letter symbols - commonly used for
comparing amino acid sequences of proteins:
R  -Carbon Atom ➢ Usually the first letter of the name
➢ When more than one amino acid has the
H2N C COOH same letter the most abundant amino acid
gets the 1st letter.
-Carboxyl
-Amino H
Group - Both types of abbreviations are given in the
Group
following slides.
- All amino acids differ from one another by their
R-groups.
- Standard amino acids are divided into four
groups based on the properties of R-groups are
non-polar.
NON-POLAR AMINO ACIDS: POLAR ACIDIC AND BASIC AMINO ACIDS:

POLAR NEUTRAL AMINO ACIDS:

 CHIRALITY AND AMINO ACIDS ACIDS-BASE PROPERTIES OF AMINO ACIDS
- Four different groups are attached to the a- - In pure form amino acids are white crystalline
carbon atom in all of the standard amino solids.
acids except glycine. - Most amino acids decompose before they melt.
➢ In glycine R-group is hydrogen - Not very soluble in water
- Therefore 19 of the 20 standard amino acids - Exists as Zwitterion: An ion with + (positive) and
contain a chiral center. – (Nagetive) charges on the same molecule with
- Chiral centers exhibit enantiomerism (left- and a net zero charge
right-handed forms). ➢ Carboxyl groups give-up a proton to get
- Each of the 19 amino acids exist in left and negative charge.
right-handed forms. ➢ Amino groups accept a proton to become
positive.

- The amino acids found in nature as well as in

proteins are L isomers.
➢ Bacteria do have some D-amino acids
➢ With monosaccharides nature favors D-
isomers. - Amino acids in solution exist in three different
- The rules for drawing Fischer projection species (zwitterions, positive ion, and negative
formulas for amino acid structures ion) - Equilibrium shifts with change in pH.
- The — COOH group is put at the top, the R group
at the bottom to position the carbon chain - Isoelectric point (pI) – pH at which the
vertically concentration of Zwitterion is maximum -- net
- The — NH2 group is in a horizontal position. charge is zero
➢ Positioning — NH2 on the left - L isomer ➢ Different amino acids have different
➢ Positioning — NH2 on the right - D isomer. isoelectric points.
➢ At isoelectric point - amino acids are not
attracted towards an applied electric field
because they net zero charge.
COOH COO- COO-
+ +
H3N C H H3N C H H2N C H

CH3 CH3 CH3

Low pH High pH
Zwitter Ion
(net + charge) (net neutral charge) (net - charge)

Neutral pH
 CYSTEIN: A CHEMICALLY UNIQUE AMINO ACID OH
N-terminal end
- Cysteine: the only standard amino acid with a O O CH2 O
sulfhydryl group ( — SH group). +H
H H
3N CH C N CH C N CH C O-
- The sulfhydryl group imparts cysteine a
chemical property unique among the standard CH3 CH2 C-terminal end

amino acids.
- Cysteine in the presence of mild oxidizing
agents dimerizes to form a cystine molecule.
➢ Cystine - two cysteine residues linked via a
Alanine Phenylalanine Serine
covalent disulfide bond.

PEPTIDE NOMENCLATURE
- The C-terminal amino acid residue keeps its
full amino acid name.
- All of the other amino acid residues have names
that end in -yl. The -yl suffi x replaces the -ine or
-ic acid ending of the amino acid name, except
for tryptophan, for which -yl is added to the
name.
- The amino acid naming sequence begins at the
N-terminal amino acid residue.
- Example:
➢ Ala-leu-gly has the IUPAC name of
alanylleucylglycine

ISOMERIC PEPTIDES
PEPTIDES - Peptides that contain the same amino acids
- Under proper conditions, amino acids can but present in different order are different
bond together to produce an unbranched molecules (constitutional isomers) with
chain of amino acids. different properties.
- The length of the amino acid chain can vary ➢ For example, two different dipeptides can
from a few amino acids to many amino acids. be formed between alanine and glycine.
- Such a chain of covalently-linked amino acids is - The number of isomeric peptides possible
called a peptide. increases rapidly as the length of the peptide
- The covalent bonds between amino acids in a chain increases.
peptide are called peptide bonds.

• Dipeptide: bond between two amino acids

• Oligopeptide: bond between ~ 10 - 20 amino
acids.
• Polypeptide: bond between large number of
amino acids.
• Every peptide has an N-terminal end and a C-
terminal end.
• +
H3N-aa-aa-aa-aa-aa-aa-aa-aa-aa-COO-
 BIOCHEMICALLY IMPORTANT SMALL PEPTIDES GENERAL STRUCTURAL CHARACTERISTICS OF
- Many relatively small peptides are PROTEINS
biochemically active: - General definition: A protein is a naturally-
➢ Hormones occurring, unbranched polymer in which the
➢ Neurotransmitters monomer units are amino acids.
➢ Antioxidants - Specific definition: A protein is a peptide in
- Small Peptide Hormones: which at least 40 amino acid residues are
➢ Best-known peptide hormones: oxytocin present:
and vasopressin. ➢ The terms polypeptide and protein are often
➢ Produced by the pituitary gland used interchangeably used to describe a
➢ nonapeptide (nine amino acid residues) protein.
with six of the residues held in the form of a ➢ Several proteins with >10,000 amino acid
loop by a disulfide bond formed between residues are known.
two cysteine residues ➢ Common proteins contain 400–500 amino
acid residues.
➢ Small proteins contain 40–100 amino acid
residues
- More than one peptide chain may be present
in a protein:
- Monomeric : A monomeric protein contains
one peptide chain.
Small Peptide Neurotransmitters: - Multimeric: A multimeric protein contains
- Enkephalins are pentapeptide more than one peptide chain.
neurotransmitters produced by the brain and
bind receptor within the brain PROTEIN CLASSIFICATION BASED ON CHEMICAL
- Help reduce pain COMPOSITION:
- Best-known enkephalins: - Simple proteins: A protein in which only
➢ Met-enkephalin: Tyr–Gly–Gly–Phe–Met amino acid residues are present:
➢ Leu-enkephalin: Tyr–Gly–Gly–Phe–Leu ➢ More than one protein subunit may be
present but all subunits contain only amino
Small Peptide Antioxidants: acids.
- Glutathione (Glu–Cys–Gly) – a tripeptide – is - Conjugated protein: A protein that has one or
present is in high levels in most cells more non-amino acid entities (prosthetic
- Regulator of oxidation–reduction reactions. groups) present in its structure:
- Glutathione is an antioxidant and protects ➢ One or more polypeptide chains may be
cellular contents from oxidizing agents such as present.
peroxides and superoxides ➢ Non-amino acid components - may be
➢ Highly reactive forms of oxygen often organic or inorganic - prosthetic groups
generated within the cell in response to ➢ Lipoproteins contain lipid prosthetic
bacterial invasion. groups.
- Unusual structural feature – Glu is bonded to ➢ Glycoproteins contain carbohydrate
Cys through the side-chain carboxyl group. groups.
➢ Metalloproteins contain a specific metal as
prosthetic group.
 PRIMARY STRUCTURE OF PROTEINS PRIMARY STRUCTURE OF PROTEINS
FOUR TYEPS OF STRUCTURES - Proteins of the same organism always same
- Primary Structure sequence (cows, pigs, etc.)
- Secondary Structure - Different sources: Insulin from pigs, cows,
- Tertiary Structure sheep, humans similar
- Quaternary - Some differences:
Species Chain A Chain B
• Primary Structure: Primary structure of protein AA #8 AA #9 AA AA #30
refers to the order in which amino acids are #10
linked together in a protein. Human Thr Ser Ile Thr
• Every protein has its own unique amino acid Pig Thr Ser Ile Ala
sequence. (porcine)
• Frederick Sanger (1953) sequenced and Cow Ala Ser Val Ala
(bovine)
determined the primary structure for the first
protein – Insulin

PRIMARY STRUCTURE OF HUMAN MYOGLOBIN - Due to differences insulin may show some
reaction over time.
- Now human insulin produced from genetically
engineered bacteria.

SECONDARY STRUCTUREOF PROTEINS

- Arrangement of atoms of backbone in space.
- The two most common types : alpha-helix (a-
helix) and the beta-pleated sheet (b-pleated
sheet).
- The peptide linkages are essentially planar thus
allows only two possible arrangements for the
peptide backbone for the following reasons:
➢ For two amino acids linked through a
peptide bond six atoms lie in the same
plane.
➢ The planar peptide linkage structure has
considerable rigidity, therefore rotation of
groups about the C–N bond is hindered.
➢ Cis–trans isomerism is possible about C–N
bond.
➢ The trans isomer is the preferred
orientation.
Alpha-helix (a-helix)
- A single protein chain adopts a shape that
resembles a coiled spring (helix):
➢ H-bonding between same amino acid
chains –intra molecular
➢ Coiled helical spring
➢ R-group outside of the helix -- not enough
room for them to stay inside
 QUATERNARY STRUCTURE OF PROTEINS
- Quaternary structure of protein refers to the
organization among the various peptide
chains in a multimeric protein:
➢ Highest level of protein organization.
➢ Present only in proteins that have 2 or more
polypeptide chains (subunits).
➢ Subunits are generally Independent of each
other - not covalently bonded.
➢ Proteins with quartenary structure are often
referred to as oligomeric proteins.
➢ Contain even number of subunits
Beta -Pleated Sheets
- Completely extended amino acid chains PROTEINS CLASSIFICATIONS BASED ON SHAPE
- H-bonding between two different chains – inter - Three types of proteins: fibrous, globular, and
and/or intramolecular membrane
- Side chains below or above the axis - Fibrous proteins: protein molecules with
elongated shape:
➢ Generally insoluble in water
➢ Single type of secondary structure
➢ Tend to have simple, regular, linear
structures.
➢ Tend to aggregate together to form
macromolecular structures, e.g., hair, nails,
etc.
- Globular proteins: protein molecules with
TERTIARY STRUCTURE OF PROTEINS peptide chains folded into spherical or globular
- The overall three-dimensional shape of a shapes:
protein. ➢ Generally water soluble – hydrophobic
- Results from the interactions between amino amino acid residues in the protein core
acid side chains (R groups) that are widely ➢ Function as enzymes and intracellular
separated from each other. signaling molecules.
- In general 4 types of interactions are observed. - Membrane proteins: associated with cell
membranes
FOUR TYPES OF INTERACTIONS ➢ Insoluble in water – hydrophobic amino acid
1. Disulfide bond: covalent, strong, between residues on the surface.
two cysteine groups ➢ Help in transport of molecules across the
2. Electrostatic interactions: Salt Bridge between membrane.
charged side chains of acidic and basic amino
acids Fibrous Proteins: Alpha-Keratin
➢ -OH, -NH2, -COOH, -CONH2 ➢ Provide protective coating for organs
3. H-Bonding between polar, acidic and/or basic ➢ Major protein constituent of hair, feather,
R groups nails, horns and turtle shells
➢ For H-bonding to occur, the H must be ➢ Mainly made of hydrophobic amino acid
attached on O, N or F residues
4. Hydrophobic interactions: Between non-polar ➢ Hardness of keratin depends upon -S-S-
side chains. bonds
 ➢ more –S-S– bonds make nail and bones
hard. MAJOR CATEGORIES OF PROTEINS BASED ON
Fibrous Proteins: Collagen FUNCTION:
➢ Most abundant proteins in humans (30% • Catalytic proteins: Enzymes are best
of total body protein) known for their catalytic role.
➢ Major structural material in tendons, • Almost every chemical reaction in the body
ligaments, blood vessels, and skin is driven by an enzyme.
➢ Organic component of bones and teeth
• Defense proteins: Immunoglobulins or
➢ Predominant structure - triple helix
antibodies are central to functioning of the
➢ Rich in proline (up to 20%) – important to
body’s immune system.
maintain structure.
• Transport proteins: Bind small
Globular Proteins: Myoglobulin biomolecules, e.g., oxygen and other
➢ An oxygen storage molecule in muscles. ligands, and transport them to other
➢ Monomer - single peptide chain with one locations in the body and release them on
heme unit. demand.
➢ Binds one O2 molecule
• Messenger proteins: transmit signals to
➢ Has a higher affinity for oxygen than
coordinate biochemical processes
hemoglobin.
between different cells, tissues, and
➢ Oxygen stored in myoglobin molecules
organs.
serves as a reserve oxygen source for
• Insulin and glucagon - regulate
working muscles.
carbohydrate metabolism.
• Human growth hormone – regulate body
Globular Proteins: Hemoglobin
growth.
➢ An oxygen carrier molecule in blood
➢ Transports oxygen from lungs to tissues
• Contractile proteins: Necessary for all
➢ Tetramer (four peptide chains) - each
forms of movement.
subunit has a heme group.
– Muscles contain filament-like
➢ Can transport up to 4 oxygen molecules at
contractile proteins (actin and
time.
myosin).
➢ Iron atom in heme interacts with oxygen
– Human reproduction depends on
the movement of sperm – possible
PROTEIN CLASSIFICATION BASED ON FUNCTION because of contractile proteins.
• Proteins play crucial roles in most • Structural proteins: Confer stiffness and
biochemical processes. rigidity
• The diversity of functions exhibited by – Collagen is a component of
proteins far exceeds the role of other cartilage a
biochemical molecules – Keratin gives mechanical strength
• The functional versatility of proteins stems as well as protective covering to
from: hair, fingernails, feathers, hooves,
• Ability to bind small molecules specifically etc.
and strongly • Transmembrane proteins: Span a cell
• Ability to bind other proteins and form fiber- membrane and help control the movement
like structures, and of small molecules and ions.
• Ability integrated into cell membranes – Have channels – help molecules
can enter and exist the cell.
 – Transport is very selective - allow ➢ Egg white - a concentrated solution of
passage of one type of molecule or protein albumin - forms a jelly when heated
ion. because the albumin is denatured
• Storage proteins: Bind (and store) small - Cooking:
molecules. ➢ Denatures proteins – Makes it easy for
– Ferritin - an iron-storage protein - enzymes in our body to hydrolyze/digest
saves iron for use in the protein.
biosynthesis of new hemoglobin ➢ Kills microorganisms by denaturation of
molecules. proteins.
– Myoglobin - an oxygen-storage ➢ Fever: >104ºF – the critical enzymes of the
protein present in muscle body start getting denatured.
• Regulatory proteins: Often found
“embedded” in the exterior surface of cell Glycoproteins
membranes - act as sites for receptor - Conjugated proteins with carbohydrates
molecules linked to them:
– Often the molecules that bind to ➢ Many of plasma membrane proteins are
enzymes (catalytic proteins), glycoproteins.
thereby turning them “on” and “off,” ➢ Blood group markers of the ABO system are
and thus controlling enzymatic also glycoproteins.
action. ➢ Collagen and mmunoglobulins are
• Nutrient proteins: Particularly important in glycoproteins.
the early stages of life - from embryo to - Collagen – glycoprotein
infant. ➢ Most abundant protein in human body (30%
– Casein (milk) and ovalalbumin (egg of total body protein)
white) are nutrient proteins ➢ Triple helix structure
– Milk also provide immunological ➢ Rich in 4-hydroxyproline (5%) and 5-
protection for mammalian young. hydroxylysine (1%) — derivatives
➢ Some hydroxylysines are linked to glucose,
PROTEIN HYDROLYSIS galactose, and their disaccharides – help in
• Hydrolysis of proteins - reverse of peptide aggregation of collagen fibrils.
bond formation:
IMMUNOGLOBULINS
- Results in the generation of an amine and a
- Glycoproteins produced as a protective
carboxylic acid functional groups.
response to the invasion of microorganisms
- Digestion of ingested protein is enzyme-
or foreign molecules - antibodies against
catalyzed hydrolysis.
antigens.
- Free amino acids produced are absorbed into
- Immunoglobulin bonding to an antigen via
the bloodstream and transported to the liver for
variable region of an immunoglobulin occurs
the synthesis of new proteins.
through hydrophobic interactions, dipole –
- Hydrolysis of cellular proteins and their
dipole interactions, and hydrogen bonds.
resynthesis is a continuous process.
LIPOPROTEINS
PROTEIN DENATURATION - Lipoprotein: a conjugated protein that
- Partial or complete disorganization of contains lipids in addition to amino acids
protein’s tertiary structure - Major function - help suspend lipids and
- Cooking food denatures the protein but does transport them through the bloodstream
not change protein nutritional value - Four major classes of plasma lipoproteins:
- Coagulation: Precipitation (denaturation of
proteins)
➢ Chylomicrons: Transport dietary
triacylglycerols from intestine to liver and
to adipose tissue.
➢ Very-low-density lipoproteins (VLDL):
Transport triacylglycerols synthesized in
the liver to adipose tissue.
➢ Low-density lipoproteins (LDL): Transport
cholesterol synthesized in the liver to cells
throughout the body.
➢ High-density lipoproteins (HDL): Collect
excess cholesterol from body tissues and
transport it back to the liver for degradation
to bile acids.