Protein Structure

Collins Edward Jana, PhD

Biochemistry Division, Biomedical

Sciences Department
Learning outcomes
References
Peptides and Polypeptides
Proteins are Polypeptides
Proteins bury hydrophobic residues in
their core
Peptides and Polypeptides
Levels of Protein Structure
Levels of Protein Structure
Primary Structure
Primary Structure
Protein Folding
Molecular chaperones
Degradation of misfolded protein
2. Secondary Structure
The  helix structure
The helix structure
The pleated sheets
The pleated sheets
 The pleated sheets
Anti-parallel -sheet

Hydrogen bonds between NH & CO grps connect

each amino acid to a single amino acid on
adjacent strand, stabilizing the structure
The pleated sheets
Mixed -sheet
 The pleated sheets
In the case of anti-parallel β-sheet, the polypeptide
makes tight “β-turns” or “hair pin” bends to fold the
chain back on itself.

β-Turns and bends: short segments of AAs that join

2 units of 2o structure
β turn or β bend involves 4 aminoacyl residues, in
which the first residue is H-bonded to the 4 th resulting
in a 180° turn
Proline & Glycine are often present in β turns
β-turn or bends
 Connecting loops
These are unstructured polypeptides that connect α-
helices to β-sheets in a protein

When illustrating a protein structure, an α-helix is

represented either as a solid cylinder, or as a helical
ribbon. While β-strands are represented as broad arrows
 3.Tertiary Structure
Mixture of various 2o structures are folded up and
packed together to form a compact structure (protein
molecule).

This is largely the result of interactions of the side

chains of the amino acids, both with each other and
with the environment.

Staphylococcal nuclease
Myoglobin
 4.Quaternary Structure
Once a tertiary structure is formed, we now have a
protein molecule, & for many proteins, that is the final
Stage.

Many functional proteins have more than one such

protein molecule or protein monomer. These
monomers link together by 2o bonds.

The monomers may be the same or different, & the

resulting multi-component molecules are variously
called dimers, tetramers, or oligomers in which 2 or 4
or more monomers have combined to form one
functional protein
 Quaternary Structure
Different terms are used to describe subunit
structure. The prefixes “homo” or “hetero” are used to
describe identical or different subunits respectively,
of 2, 3, or 4 subunit proteins.

Crop protein of bacteriophage

dimer
tetramer of human hemoglobin
Forces stabilizing Protein Structure
1.Hydrogen bonding:
The hydrogen on one
molecule attached to
O or N that is attracted
to an O or N of a different
molecule

2.Ionic interactions:
-vely charged grps can interact
with +vely charged grps
Forces stabilizing Protein Structure

3.Disulphide bonds:
The –SH grps of 2 cysteine
molecules in different regions
of a protein can undergo an
oxidation reaction to form a
disulphide (-S-S-) bridge
between the 2 chains
Forces stabilizing Protein Structure
4.Hydrophobic bonds:

Hydrophobic amino acids

associate with each other to
form hydrophobic bonds