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Influence of interatomic interactions on the structure and stability of polypeptides and proteins
Author(s) -
Scheraga Harold A.
Publication year - 1981
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1981.360200912
Subject(s) - chemistry , globular protein , tripeptide , intermolecular force , crystallography , protein structure , chemical physics , stability (learning theory) , protein superfamily , computational chemistry , amino acid , molecule , biochemistry , organic chemistry , gene , machine learning , computer science
Several examples are cited to demonstrate how conformational‐energy calculations provide information about the manner in which interatomic interactions influence the structure and stability of polypeptides and proteins, and of intermolecular complexes involving these same species. These include the screw senses of α‐helical polyamino acids, helix–coil transition parameters, properties of β‐bends, and the structures of gramicidin S and of synthetic poly‐(tripeptide) models of collagen. In all of these calculations, the multiple‐minimum problem has been surmounted. A description is provided as to how the multiple‐minimum problem is being approached in calculations on globular proteins. These computational methods have also been applied to protein structure refinement and to the calculation of structures of homologous proteins and of enzyme–substrate complexes.