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Vibrational CD of the amide II band in some model polypeptides and proteins

✍ Scribed by Vijai P. Gupta; Timothy A. Keiderling


Publisher
Wiley (John Wiley & Sons)
Year
1992
Tongue
English
Weight
834 KB
Volume
32
Category
Article
ISSN
0006-3525

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📜 SIMILAR VOLUMES


An analysis of the amide I mode in the v
✍ 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

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## Abstract Intensities and other spectral parameters of infrared amide I and II bands of α‐helical polypeptides in solutions have been determined for poly(γ‐benzylglutamate), poly(γ‐ethylglutamate), and polymethionine in chloroform, polylysine, poly(glutamic acid), and fibrillar protein tropomyosi

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## Abstract The intensities and other spectral parameters of the main components of infrared amide bands for the random and anti‐parallel pleated sheet forms have been determined for poly‐S‐carbobenzoxymethylcysteine, poly‐__S__‐carboxymethylcysteine, polylysine and silk fibroin of __Bombyx mori__

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## Abstract Infrared spectra of poly(D,L‐alanine), poly(L‐glutamic acid), poly(L‐lysine), silk fibroin, and tropomyosin have been registered for various conformations of the polypeptide chain. Assuming additivity of the main‐ and side‐chain absorption, spectral parameters of amide I and II absorpti

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✍ 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