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Vibrational analysis of peptides, polypeptides, and proteins. XXIV. Conformation of poly(α‐aminoisobutyric acid)
Author(s) -
Dwivedi Anil M.,
Krimm S.,
Malcolm B. R.
Publication year - 1984
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.360231016
Subject(s) - chemistry , aminoisobutyric acid , raman spectroscopy , helix (gastropod) , context (archaeology) , crystallography , molecule , amino acid residue , amino acid , peptide sequence , biochemistry , organic chemistry , optics , physics , ecology , paleontology , snail , gene , biology
Raman and polarized ir spectra have been obtained on built‐up monomolecular films of poly(α‐aminoisobutyric acid), and analyzed in the context of normal mode calculations on 3 10 ‐, α‐, and α′‐helix conformations of this molecule. The average discrepancy between observed and calculated frequencies is significantly smaller for the 3 10 ‐helix than for the other structures. This, together with the more satisfactory explanation of several special features of the spectra, indicates that this polypeptide adopts a 3 10 ‐helix conformation in such thin films.