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

✍ Scribed by S. Yu. Venyaminov; N. N. Kalnin

Publisher: Wiley (John Wiley & Sons)
Year: 1990
Tongue: English
Weight: 669 KB
Volume: 30
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360301310

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✦ Synopsis

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 α‐, β‐, and random coil conformations have been derived. The amide I band parameters for H~2~O and D~2~O have been compared.

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Quantitative IR spectrophotometry of pep

Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands

✍ S. Yu. Venyaminov; N. N. Kalnin 📂 Article 📅 1990 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 865 KB

## Abstract Infrared spectra of the amino acid residues in H~2~O solution have been obtained in the 1800–1400‐cm^−1^ region. It has been established that amino acid residues of arginine, asparagine, glutamine, aspartic and glutamic acids, lysine, tyrosine, histidine, and phenylalanine have intensiv