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Quantitative IR spectrophotometry of peptide compounds in water (H 2 O) solutions. III. Estimation of the protein secondary structure
Author(s) -
Kalnin N. N.,
Baikalov I. A.,
Venyaminov S. Yu.
Publication year - 1990
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360301311
Subject(s) - globular protein , chemistry , protein secondary structure , crystallography , infrared spectroscopy , helix (gastropod) , peptide , infrared , spectrophotometry , protein structure , analytical chemistry (journal) , chromatography , biochemistry , optics , organic chemistry , physics , ecology , snail , biology
Infrared spectra of 13 globular proteins have been obtained in the 1800–1480‐cm −1 region for H 2 O 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 β‐structure, disordered β‐structure, turns, and remainder were 0.98, 0.80, 0.99, 0.87, 0.90, and 0.92 respectively.