The Raman and ir spectra of a-helical polybglutarnic acid) have been assigned on the basis of a normal mode calculation for this structure. The force field was based on our previously refined mainchain force constants for a-polyb-alanine) and side-chain force constants for /3calcium-poly(L-glutamate
Vibrational analysis of peptides, polypeptides, and proteins. II. β-Poly(L-alanine) and β-poly(L-alanylglycine)
✍ Scribed by W. H. Moore; S. Krimm
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1976
- Tongue
- English
- Weight
- 927 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The normal vibration frequencies of poly(L‐alanine) and poly(L‐alanylglycine) in the antiparallel chain‐pleated sheet structure have been calculated, using the force field for polyglycine I from the previous paper (Biopolymers 15, 2439–2464) plus additional force constants for the methyl group. The agreement with observed ir and Raman bands is very good. This substantiates the excellent transferability of the force field, since polyglycine I was shown to have a rippled‐sheet structure. The amide I and amide II mode splittings are very well accounted for by transition dipole coupling, showing that subtle structural differences are sensitively manifested through this mechanism.
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