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Prog Biophys Mol Biol. 2001;76(1-2):1-102.

The interrelationships of side-chain and main-chain conformations in proteins.

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Department of Biochemistry, Bose Institute, P-1/12, CIT Scheme VIIM, 700 054, Calcutta, India.


The accurate determination of a large number of protein structures by X-ray crystallography makes it possible to conduct a reliable statistical analysis of the distribution of the main-chain and side-chain conformational angles, how these are dependent on residue type, adjacent residue in the sequence, secondary structure, residue-residue interactions and location at the polypeptide chain termini. The interrelationship between the main-chain (phi, psi) and side-chain (chi 1) torsion angles leads to a classification of amino acid residues that simplify the folding alphabet considerably and can be a guide to the design of new proteins or mutational studies. Analyses of residues occurring with disallowed main-chain conformation or with multiple conformations shed some light on why some residues are less favoured in thermophiles.

[Indexed for MEDLINE]

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