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Vibrational CD of polypeptides. X. A study of α‐helical oligopeptides in solution
Author(s) -
Yasui S. C.,
Keiderling T. A.,
Katakai Ryoichi
Publication year - 1987
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.360260814
Subject(s) - chemistry , helix (gastropod) , oligopeptide , amide , protein subunit , spectral line , crystallography , stereochemistry , peptide , physics , biochemistry , ecology , astronomy , snail , gene , biology
Abstract We have measured the vibrational CD (VCD) of a series of heterooligopeptides— o ‐nitrophenylsulfenyl( L ‐Met‐ L ‐Met‐ L ‐Leu) n ‐OEt, n = 6,8,10,11–in the amide A, I, and II regions. These spectra are identical in shape and magnitude, within our signal to noise limits. The VCD in each band are of exactly the shape expected for a right‐handed α‐helix and imply that VCD of the polypeptide α‐helix is relatively unaffected by chain length down to the 18‐subunit level.