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|Title:||The Nuclear Magnetic Resonance Study of Lipid Protein Interactions in Model Membrane Systems|
|Author(s):||Rice, David Morrison|
|Department / Program:||Chemistry|
|Degree Granting Institution:||University of Illinois at Urbana-Champaign|
|Abstract:||The nuclear magnetic resonance spectrum of deuterium is a useful probe of the state of acyl chain order and rate of motion in bilayer membranes. In order to determine the effect of membrane protein upon the state of lipid motion, a variety to deuterium labeled phosphatidylcholines have been synthesized and these have been reconstituted with several membrane proteins and peptides. The proteins include gramicidn A', cytochrome C oxidase (E.C. 220.127.116.11), sarcoplasmic reticulum Ca('+2), Mg('+2) ATPase (E.C. 18.104.22.168), human brain myelin apoprotein, lipophillin, and f(,1) phage coat protein.
The deuterium magnetic resonance spectra of these complexes have shown that membrane protein neither orders nor completely immobilizes acyl chain motion. These results have been reconciled with nitroxide electron spin resonance results by noting the time scale differences between the two techniques. Only the fastest acyl chain motions are hindered by the protein surface. Phosphorus-31 results have indicated that there might be some slow motional component in the head group. The phosphorus spectrum of lipids is motionally broadened by protein. At low concentrations gramicidn A' has on ordering effect similar to cholesterol, but this ordering is probably irrelevant to biological membranes. Preliminary experiments have been begun using a deuterated nitroxide labeled phospholipid. A procedure is described for the synthesis of high yield, and experiments with gramicidin, while hindered by paramagnetic broadening, show that at the 2 position of the acyl chain there is little nitroxide perturbation.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1980.
|Date Available in IDEALS:||2014-12-13|