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IR (vibrational) CD of peptide β‐turns: A theoretical and experimental study of cyclo ‐(‐Gly‐Pro‐Gly‐ D ‐Ala‐Pro‐)
Author(s) -
Wyssbrod Herman R.,
Diem Max
Publication year - 1992
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.360320912
Subject(s) - chemistry , pentapeptide repeat , random coil , peptide , molecule , cyclic peptide , stereochemistry , vibrational circular dichroism , spectral line , infrared spectroscopy , crystallography , circular dichroism , organic chemistry , physics , biochemistry , astronomy
IR vibrational CD (VCD) has been observed for the cyclic pentapeptide cyclo ‐(‐Gly‐Pro‐Gly‐ D ‐Ala‐Pro‐) in solution in CDBr 3 . The observed VCD spectra do not resemble the VCD features of any of the previously reported peptide secondary structures, such as α‐helical, “random coil,” or sheet structures, and might be due to the β‐turn contained in this molecule. To shed light onto the origin of the observed spectra, VCD intensity calculations, based on the solution and solid‐state structures of cyclo ‐(‐Gly‐Pro‐Gly‐D‐Ala‐Pro‐), have been carried out. In addition, calculated VCD data for pure β‐turns are discussed. © 1992 John Wiley & Sons, Inc.