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Proceedings Paper

FT-IR Studies Of Lipid/Protein Interaction In Biological Membranes
Author(s): Richard Mendelsohn; Mark Jaworsky; Gloria Anderle
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Paper Abstract

FT-IR spectroscopy has been used to monitor phospholipid order and melting characteristics as well as protein secondary structure in reconstituted membrane systems. The protein used in the current work is CaATPase, a Calcium-pumping protein isolated from rabbit skeletal muscle. The protein is isolated, purified and reconstituted into phospholipid vesicles of the desired composition. High precision (0.03 cm-1) measurements of the temperature dependence of the acyl chain CH2 stretching frequencies are used to construct melting curves for the various phospholipids used in the current work. The effect of CaATPase on lipid order depends upon the level of unsaturation of the lipid acyl chains, the strongest perturbations being observed for molecules containing one saturated and one unsaturated chain. Use of acyl chain perdeuterated lipids as one component of a binary lipid mixture permits studies of the thermal response of each component in either binary lipid mixtures or ternary complexes composed of two lipids plus protein. The tendencies of this integral membrane protein to preferentially interact with a particular lipid component is noted in several instances.

Paper Details

Date Published: 20 December 1985
PDF: 2 pages
Proc. SPIE 0553, Fourier and Computerized Infrared Spectroscopy, (20 December 1985); doi: 10.1117/12.970749
Show Author Affiliations
Richard Mendelsohn, Rutgers University (United States)
Mark Jaworsky, Rutgers University (United States)
Gloria Anderle, Rutgers 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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