BIOLOGY FORM 4

Chapter 4: Proteins
Chapter 4: Proteins

CONTENTS
INTODUCTION
PROTEIN STRUCTURES
TYPES OF AMINO ACIDS
SOURCES OF REFERENCE

INTRODUCTION

A protein is a linear polymer built from about 20 different

amino acids. The type and the sequence of amino acids in a
protein are specified by the DNA in the cell that produces them.
This sequence of amino acids is essential since it determines the
overall structure and function of a protein.

Protein

Functions

Antibodies
are specialized
proteins involved
in defending the
body from
antigens (foreign
invaders).

Contractile
Proteins
are responsible
for movement.
Examples
include actin and
myosin.

Enzymes

Hormonal
Proteins

Structural
Proteins

are proteins
that facilitate
biochemical
reactions.
They are
often referred
to as
catalysts
because they
speed up
chemical
reactions.

- are
messenger
proteins
which help to
coordinate
certain bodily
activities.
Examples
include
insulin,
oxytocin, and
somatotropin.

are fibrous
and stringy
and provide
support.
Examples
include
keratin,
collagen, and
elastin.

Storage Proteins

Transport Proteins

- store amino acids.

Examples include
ovalbumin and casein.
Ovalbumin is found in
egg whites and casein
is a milk-based
protein.

are carrier proteins

which move molecules
from one place to
another around the
body. Examples
include hemoglobin
and cytochromes.

Transport Proteins are carrier proteins

which move molecules
from one

PROTEIN STRUCTURES

Primary Structure of Proteins

The primary structure of peptides and proteins refers to the linear
number and order of the amino acids present. The convention for the
designation of the order of amino acids is that the N-terminal end
(i.e. the end bearing the residue with the free -amino group) is to
the left (and the number 1 amino acid) and the C-terminal end (i.e.
the end with the residue containing a free -carboxyl group) is to the
right.

Secondary

Structure in Proteins
The ordered array of amino acids in a protein confer regular
conformational forms upon that protein. These
conformations constitute the secondary structures of a
protein. In general proteins fold into two broad classes of
structure termed, globular proteins or fibrous proteins.
Globular proteins are compactly folded and coiled, whereas,
fibrous proteins are more filamentous or elongated. It is the
partial double-bond character of the peptide bond that
defines the conformations a polypeptide chain may assume.
Within a single protein different regions of the polypeptide
chain may assume different conformations determined by
the primary sequence of the amino acids.

Tertiary

Structure of Proteins
Tertiary structure refers to the complete three-dimensional
structure of the polypeptide units of a given protein. Included in
this description is the spatial relationship of different secondary
structures to one another within a polypeptide chain and how
these secondary structures themselves fold into the threedimensional form of the protein. Secondary structures of proteins
often constitute distinct domains. Therefore, tertiary structure
also describes the relationship of different domains to one
another within a protein. The interactions of different domains is
governed by several forces: These include hydrogen bonding,
hydrophobic interactions, electrostatic interactions and van der
Waals forces.

Quaternary

Structure
Many proteins contain 2 or more different polypeptide chains that are
held in association by the same non-covalent forces that stabilize the
tertiary structures of proteins. Proteins with multiple polypetide chains
are oligomeric proteins. The structure formed by monomer-monomer
interaction in an oligomeric protein is known as quaternary structure.
Oligomeric proteins can be composed of multiple identical polypeptide
chains or multiple distinct polypeptide chains. Proteins with identical
subunits are termed homo-oligomers. Proteins containing several distinct
polypeptide chains are termed hetero-oligomers.
Hemoglobin, the oxygen carrying protein of the blood, contains two
and two subunits arranged with a quaternary structure in the form,
22. Hemoglobin is, therefore, a hetero-oligomeric protein.

TYPES OF AMINO ACIDS

Amino acids is an organic compound containing an amino group (NH2), a

carboxylic acid group (COOH), and any of various side groups, especially
any of the 20 compounds that have the basic formula NH2CHRCOOH, and
that link together by peptide bonds to form proteins or that function as
chemical messengers and as intermediates in metabolism.
There are twenty kinds of amino acids that support the body, each having
their own functions.

20

Types Of Amino Acids

SOURCES OF REFERENCE

http://biology.about.com/od/molecularbiology/a/aa101904a.htm

http://www.biology-online.org/dictionary/Protein

http://themedicalbiochemistrypage.org/protein-structure.html

http://www.hornetjuice.com/amino-acids-types.html

THANK
.

YOU