## 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
Intensities and other spectral parameters of infrared amide bands of polypeptides in the β- and random forms
✍ Scribed by Yu. N. Chirgadze; B. V. Shestopalov; S. Yu. Venyaminov
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 743 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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 in heavy water solutions and in organic solvents. Assuming that the optical spectra of these two types of structure are additive, the method was proposed for determining relative contents and molar absorption coefficients of amide I band. Integral intensity and maximum frequency values of the main components of the amide I band for all the samples in the β‐form turned out to be specific. In contrast to this the integral intensity of the band of amide I in the random coil form varied within certain limits, while the main maximum frequency for all samples remained the same.
📜 SIMILAR VOLUMES
## 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