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Vibrational analysis of peptides, polypeptides, and proteins. I. Polyglycine I
Author(s) -
Moore W. H.,
Krimm S.
Publication year - 1976
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.1976.360151210
Subject(s) - antiparallel (mathematics) , chemistry , amide , dipole , force field (fiction) , hydrogen bond , computational chemistry , beta sheet , chemical physics , normal mode , crystallography , molecular physics , protein structure , molecule , vibration , organic chemistry , physics , biochemistry , quantum mechanics , magnetic field
A force field has been refined for the antiparallel chain‐rippled sheet structure of polyglycine I. Transition dipole coupling and hydrogen bonding are explicitly taken into account. Amide I and amide II mode splittings are well accounted for, the latter also providing a quantitative explanation of the amide A and amide B mode frequencies and intensities. In addition to predicting other features of the vibrational spectrum of polyglycine I, this force field is completely transferable to other β polypeptides, even though these have the antiparallel chainpleated sheet structure.