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Proceedings Paper

Fourier Transform Vibrational Circular Dichroism In The amide I band Of Polypeptides
Author(s): M. Germana Paterlini; Teresa B. Freedman; Laurence A. Nafie
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Paper Abstract

The Fourier transform vibrational circular dichroism (VCD) in the amide I region of poly-L-lysine in D20 solution has been investigated. Signals corresponding to the random coil, a-helix and antiparallel (3-sheet have been characterized. The spectrum of the a-helix shows the presence of three distinct features in agreement with previous results on deuterated polypeptides. We were able to detect the antiparallel β-sheet conformation in solution; the signal is unexpectedly large and monosignate in contrast to that predicted from exciton theory.

Paper Details

Date Published: 20 December 1985
PDF: 2 pages
Proc. SPIE 0553, Fourier and Computerized Infrared Spectroscopy, (20 December 1985); doi: 10.1117/12.970806
Show Author Affiliations
M. Germana Paterlini, Syracuse University (United States)
Teresa B. Freedman, Syracuse University (United States)
Laurence A. Nafie, Syracuse University (United States)

Published in SPIE Proceedings Vol. 0553:
Fourier and Computerized Infrared Spectroscopy
David G. Cameron; Jeannette G. Grasselli, Editor(s)

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