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Characterization of β‐bend ribbon spiral forming peptides using electronic and vibrational CD
Author(s) -
Yoder Gorm,
Keiderling Timothy A.,
Formaggio Fernando,
Crisma Marco,
Toniolo Claudio
Publication year - 1995
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.360350111
Subject(s) - ribbon , chemistry , amide , fourier transform infrared spectroscopy , polarity (international relations) , crystallography , spectral line , fourier transform , infrared spectroscopy , oligopeptide , helix (gastropod) , characterization (materials science) , stereochemistry , peptide , organic chemistry , optics , nanotechnology , materials science , mathematical analysis , ecology , biochemistry , physics , mathematics , astronomy , biology , snail , composite material , cell
Abstract Terminally blocked (L‐Pro‐Aib) n and Aib‐(L‐Pro‐Aib) n sequential oligopeptides are known to form right‐handed β‐bend ribbon spirals under a variety of experimental conditions. Here we describe the results of a complete CD and ir characterization of this subtype of 3 10 ‐helical structure. The electronic CD spectra were obtained in solvents of different polarity in the 260‐180 nm region. The vibrational CD and Fourier transform ir (FTIR) spectra were measured in deuterochloroform solution in the amide I and amide II (1750‐1500 cm −1 ) regions. The critical chain length for full development of the β‐bend ribbon spiral structure is found to be five to six residues. Spectral effects related to concentration‐induced stabilization of the structures of the longer peptides were seen in the resolution‐enhanced FTIR spectra. Comparison to previous studies of (Aib) n and (Pro) n oligomers indicate that the low frequency of the amide I mode is due to the interaction of secondary and tertiary amide bonds and not to a strong difference in conformation from a regular 3 10 ‐helix. © 1995 John Wiley & Sons, Inc.