SCHOOL OF POST GRADUATE STUDIES

DEPARTMENT OF CHEMISTRY
PRESENTATION ON ADVANCED BIOCHEMISTRY
TITLE: STRUCTURE AND FUNCTION OF PROTEINS,
DEPENDENCE OF PROTEIN FUNCTION ON STRUCTURE

PREPARED BY: MUDIN JEMAL ,2 016

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BIOCHEM.PRESENTATION 1
 INTRODUCTION

What Are Proteins?

• Large molecules
• Made up of chains of amino acids
• Are found in every cell in the body

• Are involved in most of the body’s functions and life

processes
• The sequence of amino acids is determined by DNA
• A protein is usually composed of 50 to 400+ amino acids.

BIOCHEM.PRESENTATION 2
 STRUCTURE OF PROTEINS
• The four levels of protein structure are
illustrated in Figure below

Primary Assembly
STRUCTURE

PROCESS
Folding
Secondary

Packing
Tertiary
Interaction

Quaternary
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BIOCHEM.PRESENTATION
1. Primary Structure :result from protein assembly that
occurs at ribosome
• linear
• ordered
• 1 dimensional
• sequence of amino acid
polymer
• by convention, written
from amino end to
carboxyl end
• a perfectly linear amino
acid polymer is neither
functional nor
energetically favorable 
folding!

BIOCHEM.PRESENTATION 4
• 2.Secondary Structure: results from protein folding of
localized spatial interaction among primary structure elements
(amino acids ).

• non-linear
• 3 dimensional
• localized to regions of an amino acid chain
• formed and stabilized by hydrogen bonding,
electrostatic and van der Waals interactions

BIOCHEM.PRESENTATION 5
• Types of secondary structures

α-helix β-sheet

Secondary structures, α-helix and β-sheet,

have regular hydrogen-bonding patterns.

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 α-helix β-sheet
- the basic unit of a
- alpha helices are about beta-sheet is called a
10 residues on average beta-strand

- side chains are well - unlike alpha-helix, sheets

staggered, preventing can be formed from
steric hindrance discontinuous regions of a
polypeptide chain

- beta-sheets can form

- helices can form various higher-level
bundles, coiled coils, etc. structures, such as a
beta-barrel

BIOCHEM.PRESENTATION 7
3.Tertiary Structure: results from protein packing

 Spatial arrangement of various secondary

structures (relationship of domains); the complete
3-D structure of polypeptide units

 hydrogen bonding, hydrophobic interactions,

electrostatic interactions, van der Waals’ forces
all stabilize conformation

 For many proteins, tertiary is the highest level of

structure

BIOCHEM.PRESENTATION 8
 4.Quaternary Structure:

refers to the number of subunits, their relative

positions, and contacts between the individual
monomers in a multimeric protein

due to the protein interaction among the tertiary

structure element of separate polymer chains

Non linear
3-dimensional

BIOCHEM.PRESENTATION 9
 Hierarchical nature of protein structure

Primary structure (Amino acid sequence)

↓
Secondary structure （ α-helix, β-sheet ）
↓
Tertiary structure （ Three-dimensional structure
formed by assembly of secondary structures ）
↓
Quaternary structure （ Structure formed by more
than one polypeptide chains ）

BIOCHEM.PRESENTATION 10
 FUNCTION OF PROTEINS

• Functions of proteins are:

– Provide structural and mechanical support
– Maintain body tissues
– Functions as enzymes and hormones
– Help maintain acid base balance
– Transport nutrients
– Assist the immune system
– Serve as a source of energy when necessary

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 ROLES OF PROTEINS

• Structural and mechanical support: proteins are the body’s

building materials, providing strength and flexibility to tissues,
ligaments, muscles, bones nails, hairs and skins.
• Enzymes and hormones: they are needed to make most
enzymes that speed up reactions in the body and many
hormones that direct specific activities.
• Fluid balance : they play a major role in ensuring the body
fluids are evenly dispersed in the body.
BIOCHEM.PRESENTATION 12
• Acid-base balance: act as buffers to help keep the pH of the body
fluids.
• Transport: they shuttle substance such as oxygen, waste
products and nutrients.
• Antibodies and immune : create specialized antibodies that
attack pathogens.
• Energy: they provide 4 calorie per gram , so used as fuel .
• Protein plays many important roles in the body,
including:
– Helping facilitate muscular contraction
– Promoting and appetite control

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 DEPENDENCE OF PROTEIN FUNCTION ON
STRUCTURE

• Protein function depends on both

– amino acid content, and
– amino acid sequence.
• Protein fold into diverse shapes such as
– spherical
– elipsoidal
– long strands, etc.
• All information for 3-D structure is contained
in the linear sequence of amino acids.
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• Any alteration in the structure or sequencing
changes the shape and function of the
protein
• Alteration of the protein’s shape and thus
functions through the use of
– Heat
– Acids
– Bases
– Salts
– Mechanical agitation
• Primary structure is unchanged by denaturing
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 Protein denaturants
• • high temperatures
• - cause protein unfolding, aggregation

• • low temperatures
• - some proteins are sensitive to cold denaturation

• • heavy metals (e.g., lead, cadmium, etc.)

• - highly toxic; efficiently induce the ‘stress response’

• • proteotoxic agents (e.g., alcohols, cross-linking agents, etc.)

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• oxygen radicals, ionizing radiation
- cause permanent protein damage
chaotropes (urea, guanidine hydrochloride, etc.)
- highly potent at denaturing proteins;
often used in protein folding studies
•The chemical characters of the amino-acid side chains
have important consequences for the way they
participate in the folding and functions
of proteins

BIOCHEM.PRESENTATION 17
•The amino-acid side chains have different tendencies to
participate in interactions with each other and with water.
These differences profoundly influence their contributions to
protein stability and to protein function.

BIOCHEM.PRESENTATION 18
 SUMMARY
• Proteins are key players in our living systems.
• Proteins are polymers consisting of 20 kinds of amino acids.
• Each protein folds into a unique three-dimensional structure
defined by its amino acid sequence.
• Protein structure has a hierarchical nature.
• Protein structure is closely related to its function.

Four levels of protein structure:

Primary structure
Secondary structure
Tertiary structure
Quaternary structure
BIOCHEM.PRESENTATION 19
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