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Proceedings Paper

Visible and UV Raman spectroscopy of membrane-bound peptides
Author(s): Hideo Takeuchi; Teruhiko Maruyama; Yoshikazu Ohtsuka; Issei Harada
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Paper Abstract

Two Raman spectroscopic methods are presented to investigate the structures of membrane- bound peptides. In the first method, water accessibility to each tryptophan side chain of gramicidin A incorporated into phospholipid liposomes has been measured by use of hydrogen-deuterium exchange, selective isotopic labeling, and visible Raman spectroscopy. The water accessibility data are best explained by a newly proposed ion channel structure of gramicidin A. In the second method, we utilize ultraviolet resonance Raman intensity as a probe of environments of aromatic residues. Application of this method to enkephalin has shown that the tyrosine side chain is buried in the hydrophobic region of the lipid membrane while the phenylalanine side chain is not.

Paper Details

Date Published: 17 June 1993
PDF: 6 pages
Proc. SPIE 1921, Laser Spectroscopy of Biomolecules, (17 June 1993); doi: 10.1117/12.146140
Show Author Affiliations
Hideo Takeuchi, Tohoku Univ. (Japan)
Teruhiko Maruyama, Tohoku Univ. (Japan)
Yoshikazu Ohtsuka, Tohoku Univ. (Japan)
Issei Harada, Tohoku Univ. (Japan)

Published in SPIE Proceedings Vol. 1921:
Laser Spectroscopy of Biomolecules
Jouko E. Korppi-Tommola, Editor(s)

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