The interrelationships of side-chain and main-chain conformations in proteins.
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.
Chakrabarti
P
P
Department of Biochemistry, Bose Institute, P-1/12, CIT Scheme VIIM, 700 054, Calcutta, India. boseinst.ernet.in
Pal
D
D
D018360:Crystallography, X-Ray / Q000379:methods; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D013329:Structure-Activity Relationship
D010455:Peptides; D011506:Proteins; D011994:Recombinant Proteins