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- W2113671566 abstract "An analysis of a non-redundant set of protein structures from the Brookhaven Protein Data Bank has been carried out to find out the residue preference, local conformation, hydrogen bonding and other stabilizing interactions involving cis peptide bonds. This has led to a reclassification of turns mediated by cis peptides, and their average geometrical parameters have been evaluated. The interdependence of the side and main-chain torsion angles of proline rings provided an explanation why such rings in cis peptides are found to have the DOWN puckering. A comparison of cis peptides containing proline and non-proline residues show differences in conformation, location in the secondary structure and in relation to the centre of the molecule, and relative accessibilities of residues. Relevance of the results in mutation studies and the cis-trans isomerization during protein folding is discussed." @default.
- W2113671566 created "2016-06-24" @default.
- W2113671566 creator A5000031273 @default.
- W2113671566 creator A5026479756 @default.
- W2113671566 date "1999-11-01" @default.
- W2113671566 modified "2023-10-16" @default.
- W2113671566 title "Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations 1 1Edited by J. M. Thornton" @default.
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- W2113671566 doi "https://doi.org/10.1006/jmbi.1999.3217" @default.
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