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Chapter 4: Proteins
Chapter 4: Proteins
CONTENTS
INTODUCTION
PROTEIN STRUCTURES
TYPES OF AMINO ACIDS
SOURCES OF REFERENCE
INTRODUCTION
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
PROTEIN STRUCTURES
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.
20
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
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