𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. III. Estimation of the protein secondary structure

✍ Scribed by N. N. Kalnin; I. A. Baikalov; S. Yu. Venyaminov

Publisher
Wiley (John Wiley & Sons)
Year
1990
Tongue
English
Weight
564 KB
Volume
30
Category
Article
ISSN
0006-3525

No coin nor oath required. For personal study only.

✦ Synopsis

Infrared spectra of 13 globular proteins have been obtained in the 1800-1480-cm-' region for H 2 0 solutions. A method for estimating protein secondary structure from the ir spectrum has been developed. The method can also be used for estimating polypeptide and fibrous protein conformation. For the globular and fibrous proteins and polypeptides analyzed, the correlation coefficients between the ir and x-ray estimates of ordered helix, disordered helix, ordered @-structure, disordered @-structure, turns, and remainder were 0.98, 0.80, 0.99, 0.87, 0.90, and 0.92 respectively.

📜 SIMILAR VOLUMES

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

Quantitative IR spectrophotometry of pep
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
✍ S. Yu. Venyaminov; N. N. Kalnin 📂 Article 📅 1990 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 669 KB

## 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