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Vibrational analysis of peptides, polypeptides and proteins. XII—fermi resonance analysis of the unperturbed ND stretching fundamental in polypeptides

✍ Scribed by S. Krimm; Anil M. Dwivedi


Publisher
John Wiley and Sons
Year
1982
Tongue
English
Weight
498 KB
Volume
12
Category
Article
ISSN
0377-0486

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📜 SIMILAR VOLUMES


Vibrational analysis of conformation in
✍ S. Krimm 📂 Article 📅 1983 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 408 KB 👁 2 views

## 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

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## 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

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✍ P. C. Painter; M. M. Coleman 📂 Article 📅 1978 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 610 KB

## Abstract 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

Vibrational analysis of peptides, polype
✍ Anil M. Dwivedi; S. Krimm 📂 Article 📅 1984 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 940 KB

## 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