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Proteins Structure & Composition: DR Mohamed Abumaree

This document summarizes protein structure and composition. It discusses that proteins have primary, secondary, tertiary, and sometimes quaternary structures. The primary structure is the linear sequence of amino acids in a polypeptide chain. Secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonds between amino acids in the chain. Tertiary structure refers to the overall 3D shape of the protein formed by interactions between amino acid side chains. Quaternary structure results from the aggregation of multiple polypeptide subunits.

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36 views24 pages

Proteins Structure & Composition: DR Mohamed Abumaree

This document summarizes protein structure and composition. It discusses that proteins have primary, secondary, tertiary, and sometimes quaternary structures. The primary structure is the linear sequence of amino acids in a polypeptide chain. Secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonds between amino acids in the chain. Tertiary structure refers to the overall 3D shape of the protein formed by interactions between amino acid side chains. Quaternary structure results from the aggregation of multiple polypeptide subunits.

Uploaded by

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LECTURE 3

Proteins Structure & Composition


Campbell & Reece; 7th Edn. Ch 5, pp. 68-80

By
Dr Mohamed Abumaree
Molecular Reproductive Biology & Immunology
College of Medicine
King Saud bin Abdulaziz University for Health Science
Riyadh
2009

1
Proteins
 Proteins have many structures

 Proteins have many functions:


1. Speed up chemical reactions (Enzyme)
2. Provide structural support
3. Storage
4. Transport
5. Cellular communications
6. Movement
7. Defense against foreign substances

2
Polypeptides
 Polypeptides are polymers constructed
from the same set of 20 amino acids

 A protein consists of one/more


polypeptides folded (doubled) & coiled
(twisting) into specific conformations

3
Amino acids
• Amino acids are
organic molecules

• 20 amino acids build


up proteins

 Alpha (α) carbon is attached to amino & carboxyl


groups, hydrogen atom & R group (different side chain)
4
 R group:

1. Hydrogen atom (glycine)


2. Carbon skeleton attached to different
functional groups (for example, glutamine)

 The physical & chemical properties of the


side chain determine the characteristics of an
amino acid

5
Glycine (Gly-G) Alanine (Ala-A)

Valine (Val - V)

6
Essential & Non-essential amino acids
 An essential amino acid cannot be synthesized by the
organism & must be supplied in the diet

 Essential amino acids: isoleucine, leucine, lysine,


methionine, phenylalanine, threonine, tryptophan and
valine

 Histidine is an essential for children

 Arginine is needed by adults suffering from liver


disease
7
 Non-essential amino acids are manufactured
by the body from other compounds

 Non-essential amino acids: alanine,


asparagine, aspartic acid, cysteine, glutamic acid,
glutamine, glycine, proline, serine, taurine &
tyrosine

 NOT obtaining enough essential amino acids


causes degradation of the body's proteins
(Muscle)
8
Human body does not store excess
amino acids unlike fat and starch

So, amino acids must be supplied


in our food daily
Amino Acids Classification
1. Non-polar (hydrophobic) amino acids

2. Polar (hydrophilic) amino acids

3. Acidic amino acids (carboxyl group; negative


charge; so hydrophilic)

4. Basic amino acids (amino group positive


charge; so hydrophilic)
10
Non-Polar Amino Acids

11
Polar Amino Acids

12
Electrically Charged
Amino Acids

13
Amino Acid Polymers

A polypeptide is a polymer of many amino acids linked


by peptide bonds in which a carboxyl group of an amino
acid is joined to an amino group of another amino acid
14
 A polypeptide chain has a free amino group (N-
terminus) at one end & a free carboxyl group (C-
terminus) at the other end
The polypeptide backbone is attached to different
kinds amino acid side chains

15
Protein Structure

Primary Tertiary
Structure Structure

Quaternary
Secondary Structure
Structure
16
Primary Structure

A chain of amino acids


Secondary Structure
 Polypeptide chains coiled (folded) in patterns that
contribute to protein’s conformation
 The folds are referred to as secondary structure of the
protein
 The secondary structure is the result of hydrogen
bonds between the repeated units of the polypeptide
backbone
 The hydrogen bonds are weak, but they are repeated
many times, so they can support the protein shape

18
α helix: a single, spiral chain of
amino acids stabilized by hydrogen
bonds between every fourth amino
acid

Amino
acids
subunits
β pleated sheet

 2 or more regions of the polypeptide chain lying side


by side are connected by hydrogen bonds between parts
of the 2 parallel polypeptide backbones

 b-Sheets are parallel/antiparallel

Amino
acids
subunits
Tertiary structure
 The tertiary structure is the final specific geometric
shape that a protein takes

 Tertiary structure refers to the three-dimensional


structure of the entire polypeptide chain

 The shape is determined by several bonds between the


"side chains" on the amino acids, & these bonds are
causing a number of folds, bends & loops in the protein
chain

21
 Four types of bonding interactions between
"side chains":

1. Hydrogen bonding
2. Salt bridges
3. Disulfide bonds
4. Non-polar hydrophobic interactions

 The function of a protein depends on its


tertiary structure

22
Quaternary Structure
 It is the protein structure that results from the
aggregation of the polypeptide subunits

 Example; hemoglobin
 Consists of 4 polypeptide subunits
 2 α chains
 2 β chains
 Both α & β subunits consist primarily of α-helical
secondary structure
24

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