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Vibrational analysis of peptides, polypeptides, and proteins. XXXII. α‐Poly( L ‐glutamic acid)
Author(s) -
Sengupta Pradeep K.,
Krimm S.
Publication year - 1985
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.360240805
Subject(s) - chemistry , alanine , side chain , glutamic acid , raman spectroscopy , amide , crystallography , force constant , amino acid , stereochemistry , molecule , polymer , biochemistry , organic chemistry , physics , optics
The Raman and ir spectra of α‐helical poly( L ‐glutamic acid) have been assigned on the basis of a normal mode calculation for this structure. The force field was based on our previously refined main‐chain force constants for α‐poly( L ‐alanine) and side‐chain force constants for β‐calcium–poly( L ‐glutamate). Despite the identical backbone α‐helical structures, significantly different frequencies are calculated, and observed, in the amide III and backbone stretch regions of α‐poly( L ‐glutamic acid), as compared with α‐poly( L ‐alanine). This clearly demonstrates the influence of side‐chain structure on mainchain vibrational modes.