PROTEIN STRUCTURE

• The 20 amino acids are joined together by

peptide bonds.
• The linear sequence contains the information
necessary to generate a protein molecule with
a unique three-dimensional shape.
• The complexity of protein structure is best
analyzed by considering the molecule in
terms of four organizational levels, namely,
primary, secondary, tertiary, and quaternary
 PRIMARY
STRUCTURE
• The sequence of amino acids in a protein
• The AA sequence must be written from the N-terminus
to the C-terminus.
• Many genetic diseases result in proteins with abnormal
amino acid sequences, (Sickle cell anemia, Glu
replaced with Val)
PEPTIDE BOND
• Peptide bonds are
responsible for
maintaining the primary
structure
• Linkage of many amino
acids through peptide
bonds results in an
unbranched chain called
a polypeptide
SECONDARY STRUCTURE OF PROTEINS
• Regular arrangements of amino acids that
are located near to each other in the linear
sequence.
• The R group has an impact on the
likelihood of secondary structure
formation
• The α-helix, β-sheet, and β-bend (β-turn)
are examples of secondary structures

An extended zigzag
conformation of
protein backbones
-PLEATED SHEET
• Protein backbones are arranged side-by-side through
H-bonds.
• H-bonds are perpendicular to the backbone direction.
• The side chains of adjacent AAs protrude in opposite
directions.
• The adjacent protein backbones can be either parallel
or anti-parallel.
-TURN
• One -turn involves four AAs. The -CO and -NH groups
of the first AA are hydrogen bonded to the -NH and -CO
groups of the fourth AA, respectively.
• The -turn reverses abruptly the direction of a protein
backbone.
• H-bonds are perpendicular to the protein backbone.
Some common structural motifs combining α-helices and/or β-sheets
TERTIARY STRUCTURE
•Protein folding attractions:
•1. Non covalent forces
•a. Inter and intrachain H
bonding
•b. Hydrophobic interactions
•c. Electrostatic attractions
(+ to - ionic attraction)
•d. Complex formation with
metal ions
•e. Ion-dipole
•2. Covalent disulfide bridges
QUATERNARY STRUCTURE
• Quaternary structure is the result of non covalent interactions
between two or more protein chains.
• Oligomers are multisubunit proteins with all or some identical
subunits.
• The subunits are called protomers.
• two subunits are called dimers
• four subunits are called tetramers
 EXAMPLE OF QUATERNARY STRUCTURE
HEMOGLOBIN 
There are 141 and
146 amino acids in the
α and β chains
of hemoglobin,
respectively. ... (As in
myoglobin, each
subunit is linked
covalently to a
molecule of heme.)
Thus, hemoglobin bind
s four O2 molecules.
TYPES OF PROTEINS
The three types of proteins are fibrous, globular,
and membrane.
A Fibrous protein is a protein with an
elongated shape. 
• Fibrous proteins provide structural
support for cells and tissues.
• α-keratin and collagen.
•
•Globular
. proteins are spherical
("globe-like") proteins and are one of
the common protein types Globular
proteins are somewhat water-soluble
unlike the fibrous or
membrane proteins.
Example is myoglobin
Essential amino acid
AN ESSENTIAL AMINO ACID, OR
INDISPENSABLE AMINO ACID, IS AN AMINO
ACID THAT CANNOT BE SYNTHESIZED
FROM SCRATCH BY THE ORGANISM FAST
ENOUGH TO SUPPLY ITS DEMAND AND
MUST THEREFORE COME FROM THE DIET.
PROTEIN MISFOLDING
• Amyloid disease
Alzheimer's disease is thought to
be caused by the abnormal build-up
of proteins in and around brain cells.
One of the proteins involved is
called amyloid, deposits of which
form plaques around brain cells. The
other protein is called tau, deposits of
which form tangles within brain cells.
PRION DISEASE
The prion protein (PrP) strongly
implicated as
 the causative agent of
transmissible spongiform
encephalopathies (TSEs),including
 Creutzfeldt-Jakob disease in
humans,
 scrapie in sheep,
 and bovine spongiform
encephalopathy in cattle (popularly
called “mad cow disease”).
RECOMMENDED B

• Lehninger’s Principles of Biochemistry

• Lippincott’s Biochemistry