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Vibrational analysis of conformation in peptides, polypeptides, and proteins
Author(s) -
Krimm S.
Publication year - 1983
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.360220130
Subject(s) - bacteriorhodopsin , chemistry , molecule , polypeptide chain , glycine , helix (gastropod) , crystallography , amino acid , biochemistry , membrane , organic chemistry , snail , biology , ecology
A vibrational force field for the polypeptide chain has been developed for normal‐mode analysis of such molecules. It can reproduce observed frequencies of known structures to within about 5 cm −1 . We review the application of this technique to conformational problems in peptides (β‐turns and their model compounds), polypeptides [the α II ‐helix and crystalline poly(glycine II)], and proteins (bacteriorhodopsin and glucagon).