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Intensities and other spectral parameters of infrared amide bands of polypeptides in the α‐helical form
Author(s) -
Chirgadze Yu. N.,
Brazhnikov E. V.
Publication year - 1974
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.1974.360130902
Subject(s) - chemistry , amide , polylysine , chloroform , infrared , helix (gastropod) , tropomyosin , infrared spectroscopy , crystallography , analytical chemistry (journal) , organic chemistry , optics , biochemistry , actin , ecology , physics , snail , biology
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 tropomyosin from rabbit muscles in heavy water. The majority of spectral parameters are characteristic. The half‐width of the amide I band was found to vary in the range of 15–40 cm −1 for different polypeptides in the different solutions. The correlation between this parameter of the amide I band and the stability of the α‐helix was estimated. A new weak band near 1537 cm −1 of unknown origin was observed for the hydrogen form of polypeptides in the α‐helical state.