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Proceedings Paper

FTIR Vibrational Circular Dichroism Of Oligopeptides Related To Polyproline
Author(s): R. K. Dukor; T. A. Keiderling
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Paper Abstract

Vibrational Circular Dichroism (VCD) data can be routinely measured by FTIR. On our FTIR VCD instrument it is possible to obtain a spectrum where baseline correction is accomplished with solvent only. Such capability is important for measuring biological systems. Several polypeptides that have been assigned to be in 'random coil' conformation all give an amide I VCD pattern which has the same sign and bandshape as poly-L-proline II but a smaller magnitude. This is consistent with a previous proposal by Tiffany & Krimm that the 'random coil' conformation of charged polypeptides actually has a significant local ordering in the form of a left-handed extended helix. To investigate this problem further we have studied the effects of temperature and chain length on the VCD bandshape of this conformational type. The latter studies were done with (Pro)n, n=2-7. Our results indicate that even at the level of (Pro)4 the VCD spectrum has the same bandshape, sign and intensity as found in the 'random coil' poly-L-glutamic acid spectrum. Data on various 'random coil' systems will be compared to the model studies we have done.

Paper Details

Date Published: 1 December 1989
PDF: 1 pages
Proc. SPIE 1145, 7th Intl Conf on Fourier Transform Spectroscopy, (1 December 1989); doi: 10.1117/12.969458
Show Author Affiliations
R. K. Dukor, University of Illinois at Chicago (United States)
T. A. Keiderling, University of Illinois at Chicago (United States)

Published in SPIE Proceedings Vol. 1145:
7th Intl Conf on Fourier Transform Spectroscopy
David G. Cameron, Editor(s)

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