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Proceedings Paper

Vibrational circular dichroism studies of 310-helical solution conformers in dehydro-peptides
Author(s): Mario J. Citra; M. Germana Paterlini; Teresa B. Freedman; Adriano Fissi; Osvaldo Pieroni
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Paper Abstract

The solution conformations of a series of pentapeptides containing the unsaturated reside dehydrophenylalanine have been investigated by infrared, vibrational circular dichroism, electronic CD and NMR spectroscopies. VCD couplets in the NH-stretching region are identified as markers for the left or right-handed helical orientation of NH bonds in these peptides.

Paper Details

Date Published: 31 January 1994
PDF: 2 pages
Proc. SPIE 2089, 9th International Conference on Fourier Transform Spectroscopy, (31 January 1994); doi: 10.1117/12.166677
Show Author Affiliations
Mario J. Citra, Syracuse Univ. (United States)
M. Germana Paterlini, Syracuse Univ. (United States)
Teresa B. Freedman, Syracuse Univ. (United States)
Adriano Fissi, Syracuse Univ. and CNR-Institute of Biophysics (Italy)
Osvaldo Pieroni, Syracuse Univ. and CNR-Institute of Biophysics (Italy)


Published in SPIE Proceedings Vol. 2089:
9th International Conference on Fourier Transform Spectroscopy
John E. Bertie; Hal Wieser, Editor(s)

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