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水中（H₂O）肽化合物的定量红外分光光度法。II. α-、β-和无规卷曲构象的多肽和纤维状蛋白质的酰胺吸收带。

Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in alpha-, beta-, and random coil conformations.

作者信息

Kalnin N N

机构信息

Institute of Protein Research, Academy of Sciences of the USSR, Puschino, Moscow Region.

出版信息

Biopolymers. 1990;30(13-14):1259-71. doi: 10.1002/bip.360301310.

DOI:10.1002/bip.360301310
PMID:1707690
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 absorption bands corresponding to alpha-, beta-, and random coil conformations have been derived. The amide I band parameters for H2O and D2O have been compared.

摘要

已记录了聚（D，L-丙氨酸）、聚（L-谷氨酸）、聚（L-赖氨酸）、丝素蛋白和原肌球蛋白在多肽链不同构象下的红外光谱。假设主链和侧链吸收具有加和性，推导了对应α-、β-和无规卷曲构象的酰胺I和酰胺II吸收带的光谱参数。比较了H2O和D2O的酰胺I带参数。

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