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Carbon (C)
Hydrogen (H)
Oxygen (O)
Nitrogen (N)
and some proteins contain Sulfur (S)
A protein is a natural polymer, made up of amino acid monomers joined together by peptide
bonds (peptide or amide linkages).
A peptide bond (peptide or amide linkage) is a covalent bond formed between the carbon of
the carboxyl group of one amino acid and the nitrogen of the amine group of another amino
acid as shown below:
H
|
-C -N-
||
O
Denaturation refers to the destruction of the three dimensional structure of a protein that
results in the loss of biological activity.
Primary Structure
Primary structure of a protein refers to the sequence of amino acids in the chain.
Proteins are made up of many amino acids, so a short-hand system has been developed to
show the primary structure of proteins.
The following diagram shows part of the primary structure of beef insulin:
Each 3 letter symbol represents an amino acid, eg, Leu stands for leucine.
Each - represents a peptide bond (peptide or amide linkage) joining the amino acids
together.
In 1954 Frederick Sanger was the first to publish a scientific paper on the sequence of a
whole protein molecule totalling 51 amino acids for which he was awarded a Nobel Prize.
Secondary Structure
Secondary structure of a protein is the shape of the protein molecule caused by hydrogen-
bonding between -C=O and -N-H groups within the chain, the two main shapes are α helix
and β sheet.
The red dotted lines show the hydrogen bonds between amino acids along the chains
maintaining the sheet structure.
Tertiary Structure
Tertiary structure of a protein is the folding and bending of the protein molecule caused by
interaction of the R groups. This interaction may be a result of hydrogen bonding, dipole-
dipole interactions, covalent bonding or ionic bonding (salt bridges) depending on
the polarity of the R groups. The -SH group in cysteine (Cys) can form disulfide links, -C-S-
S-C- , between neighbouring groups in the presence of an oxidant.
Below are two representations of parts of protein molecules showing disulfide bonds
(disulfide links) in blue resulting in the molecule folding and bending.
Quarternary Structure
Quarternary structure of a protein are the interactions between protein subunits that result
in the protein being classified as fibrous, globular or conjugated, examples of each are
shown below.
Class Comments
keratins forms hair, quills, hoofs, nails, rich in cysteine & cystine
Globular (soluble)
Class Comments
histones occur in glandular tissue & with nucleic acids, rich in lysine & arginine
Class Comments