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Chapter 3 - Protein

The document discusses protein structure and function. It begins by outlining the structure of amino acids, the basic building blocks of proteins. It then discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. Finally, it describes the two main types of proteins - fibrous proteins that are long and insoluble, and globular proteins that are compact and soluble. The document provides examples of protein functions like enzymes, transport, and structure.

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PJ1-0619 Florence Binti Istem
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53 views34 pages

Chapter 3 - Protein

The document discusses protein structure and function. It begins by outlining the structure of amino acids, the basic building blocks of proteins. It then discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. Finally, it describes the two main types of proteins - fibrous proteins that are long and insoluble, and globular proteins that are compact and soluble. The document provides examples of protein functions like enzymes, transport, and structure.

Uploaded by

PJ1-0619 Florence Binti Istem
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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BIOCHEMISTRY

CHAPTER 3
Protein

Lecture by:
D r. H e m av a t hy S u r i k u m a r a n
LECTURE OUTLINE

• Structure of Amino acid


• Essential and non-essential amino acid
• Protein structure and function
OBJECTIVES
• To illustrate the general structure of amino
acid

• To list down groups of amino acid

• To explain protein structure and function


Learning outcome

Students should be able to:

• Illustrate the general structure of amino acids


• List down groups of amino acids
• Explain the functions of protein in relation with
their structure
 large biological molecules, or macromolecules, consisting
of one or more chains of amino acid residues.
 monomer – amino acids
 general formulae:
• These amino acids contain a variety of different
functional groups:
– Alcohols (R-OH)
– Phenols (Ph-OH)
– Carboxylic acids (R-COOH)
– Thiols (R-SH)
– Amines (R-NH2)
– and others…
• Protein function depends on both
– amino acid content, and
– amino acid sequence.
Proteins
• Make up about 15% of the cell
• Have many functions in the cell
– Enzymes
– Structural
– Transport
– Motor
– Storage
– Signaling
– Receptors
– Gene regulation
– Special functions
Functions

 biological catalysts
 storage & transport
 structural components
 mechanical
 coding for cell information
 hormones/receptors
 special functions – e.g. antibody
Characteristic of Proteins
• Contain carbon, hydrogen, oxygen, nitrogen,
and sulphur

• Serve as structural components of animals

• Serve as control molecules (enzymes)

• Serve as transport and messenger molecules

• Basic building block is the amino acid


Proteins play key roles in a living
system
• Three examples of protein functions
Alcohol
dehydrogenase
– Catalysis: oxidizes alcohols
Almost all chemical reactions in a living to aldehydes or
cell are catalyzed by protein enzymes. ketones

– Transport:
Some proteins transports various
substances, such as oxygen, ions, and so Haemoglobin
carries oxygen
on.
– Information transfer:
For example, hormones. Insulin controls
the amount of
sugar in the
blood
Amino acid: Basic unit of protein

An amino acid Different side


R chains=R, determine
the properties of 20
amino acids.
NH3+ C COO-
Amino group Carboxylic

H
acid group

• Aminegroup acts like a base, tends to bepositive.


• Carboxyl group acts like an acid, tends to be negative.
• “R group is variable, from 1 atom to 20.
• Two amino acids join together to form a dipeptide.
• Adjacent carboxyl and amino groups bond together.
Structure and Properties
Amino acid:
 its number, chemical characteristics & chain sequence,
determine protein’s characteristic,
structure & function
• Polypeptide backbone is the repeating sequence of the N-
C-C-N-C-C… in the peptide bond
• The side chain or R group is not part of the backbone or
the peptide bond
Polypeptide
Backbone
Groups of amino acids:

• depend on the nature of their side-chain (R):


• Non-polar (hydrophobic)
• Polar (hydrophilic) (6)
–uncharged amino acids
• Polar/Electrically charged amino acids
–acidic (negatively charged) (2)
–basic (positively charged (3)
20 Amino Acids
Amino Acids

Hydrophilic Hydrophobic
Essential & Non-essential amino acids

• Plants and microorganisms can synthesize all of the 20


standard amino acids.

• Mammals: cannot synthesize all amino acids; obtain some


in their diet

• Essential amino acids: those that are supplied in the diet

• Non-essential amino acids: those that can be synthesized


by the organism

• Conditional amino acids are usually NOT essential, except


in times of illness and stress.
Peptide bond…
 when amino acids linked together forming peptide
 a condensation process between -carboxyl group
& -amino group whereby water is released

• peptide bond hydrolysis amino acid monomers


• Amino acids are polymerized via amide or
“peptide” bonds:

Song to enjoy: http://www.youtube.com/watch?v=QHvklS77_U0


• Copolymer of amino acids:
– a “polypeptide”

Definition:
Amino acid polymers of ≤50 amino acids are called
“polypeptides, peptides, oligopeptides, etc.”
Amino acids polymer of >50 amino acids are called
“proteins.”
Protein’s hierarchy…
 protein’s structure – very important:
many protein characteristics depend on
orientation of the protein’s molecules

classified into:
 primary structure
 secondary structure
 tertiary structure
 quaternary structure
Levels of Protein Structure

• Primary (1°) Protein Structure


– linear sequence of amino acids.
• Secondary (2°) Protein Structure
– localized regional structures
• Teritary (3°) Protein Structure
– overal shape of proteins
• Quaternary (4°) Protein Structure
– interactions between proteins
H
P I
R E
O R
T A
E R
I C
N’ H
S Y
Types of Proteins…
 fibrous & globular proteins
 fibrous protein:
hard, long (static) & fibrous; insoluble in
water
 e.g.: collagen, keratin, fibroin

 globular protein:
 compact, folded, soluble in water, groove
 e.g.: haemoglobin, enzyme, antibody
Fibrous Proteins
Fibrous proteins
• Involved in structure: tendons ligaments blood
clots
(e.g. collagen and keratin)
• Contractile proteins in movement: muscle,
microtubules
(cytoskelton, mitotic spindle, cilia, flagella)
Globular proteins
• most proteins which move around (e.g.
albumen, casein in milk)
• Proteins with binding sites:
enzymes, haemoglobin, immunoglobulins,
membrane receptor sites
Globular Proteins

• The side chains will help determine the conformation in


an aqueous solution
E.g. of fibrous (a) and globular (b), proteins
THE END

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