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Compositional dependence of spectral features in the Raman spectra of erythrocyte membranes
Author(s) -
Goheen S. C.,
Lis L. J.,
Kucuk O.,
Westerman M. P.,
Kauffman J. W.
Publication year - 1993
Publication title -
journal of raman spectroscopy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.748
H-Index - 110
eISSN - 1097-4555
pISSN - 0377-0486
DOI - 10.1002/jrs.1250240503
Subject(s) - raman spectroscopy , chemistry , membrane , circular dichroism , crystallography , spectral line , analytical chemistry (journal) , biochemistry , chromatography , physics , optics , astronomy
Abstract The Raman spectra of erythrocyte membranes in water and D 2 O were analyzed to determine the percentage of protein and lipid contributions to the amide I spectral feature. The approach of Lippert et al. [J. Am. Chem. Soc. 98, 7075 (1976)] was modified to use circular dichroism data for protein conformations of erythrocyte membranes to determine the relative lipid and protein contributions to the 1660 cm −1 spectral feature. It was determined that 69 ± 15% of the measured peak intensity was due to the protein contribution. The implication of this data to the quantity of α‐helix conformation in membrane protein of erythrocytes, and alternative approaches to determine protein conformation from Raman spectra are discussed.