## 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 t
Vibrational analysis of peptides, polypeptides, and proteins. XXXII. α-Poly(L-glutamic acid)
✍ Scribed by Pradeep K. Sengupta; S. Krimm
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1985
- Tongue
- English
- Weight
- 670 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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). Despite the identical backbone a-helical structures, significantly different frequencies are calculated, and observed, in the amide I11 and backbone stretch regions of a-poly(L-glutamic acid), as compared with apoly(L-alanine). This clearly demonstrates the influence of side-chain structure on mainchain vibrational modes.
📜 SIMILAR VOLUMES
## Synopsis A vibrational force field for the polypeptide chain has been developed for normal-mode analysis of such molecules. It can reproduce observed frequencies of known structures to within about 5 cm-l. We review the application of this technique to conformational problems in peptides (@-tur
## Abstract The α~II~‐helix (ϕ = −70.47°, ψ = −35.75°) is a structure having the same __n__ and __h__ as the (standard) α~I~‐helix (ϕ = −57.37°, ψ = −47.49°). Its conformational angles are commonly found in proteins. Using an improved α‐helix force field, we have compared the vibrational frequencie
## Abstract Poly(His‐Ala‐Glu) and poly(Lys‐Ala‐Glu) were examined by viscosity and potentiometric titration. These measurements were interpreted in terms of the hydrodynamic size of the above sequential polypeptides. Effects of polymer, size and concentration, and solution‐salt concentration were d
## Abstract The normal modes have been calculated for structures having the dihedral angles of the four β‐turns of insulin. Frequencies are predicted in the amide I region near 1652 and 1680 cm^−1^. The former overlaps the α‐helix band at 1658 cm^−1^ in the Raman spectrum, while the latter accounts