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An analysis of the amide I mode in the vibrational spectra of unordered polypeptides and proteins
Author(s) -
Painter P. C.,
Coleman M. M.
Publication year - 1978
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.1978.360171014
Subject(s) - intramolecular force , amide , chemistry , dipole , raman spectroscopy , spectral line , sequence (biology) , crystallography , mode (computer interface) , coupling (piping) , rotational–vibrational coupling , stereochemistry , molecular physics , computational chemistry , chemical physics , infrared spectroscopy , physics , organic chemistry , quantum mechanics , materials science , biochemistry , computer science , metallurgy , operating system
The difference in the observed frequency of the amide I mode between the Raman and ir spectra of many unordered polypeptides is interpreted in terms of a model in which sequences of amide groups have similar ϕ, ψ angles. The splittings due to intramolecular interactions for the infinite helices generated by all ϕ, ψ angles are calculated by assuming transition dipole coupling. The effect of finite sequence length and distortions are then considered. This hypothesis accounts for the general features of the amide I mode of unordered polypeptides.