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. 1977 Dec;74(12):5435–5439. doi: 10.1073/pnas.74.12.5435

Deuterium magnetic resonance studies of the interaction of lipids with membrane proteins.

F W Dahlquist, D C Muchmore, J H Davis, M Bloom
PMCID: PMC431752  PMID: 202955

Abstract

The deuterium magnetic resonance spectra of lipid-protein particles containing cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) isolated from beef heart mitochondria and the specifically deuterated lipid 1-(16,16,16-trideuteropalmitoyl)-2-palmitoleoyl phosphatidylcholine are presented. These reconstituted particles are of uniform lipid and protein content; however, the spectra clearly show two environments characterized by distinctly different residual quadrupolar splittings or order parameters. The less-ordered environment shows a splitting similar to but slightly less than that of the pure lipid alone at a given temperature. The more restricted environment appears to be induced by the presence of the protein. The amount of the restricted lipid is clearly temperature dependent with a 2- to 3-fold decrease in relative amount from 2 to 22 degrees. The rate of exchange of lipid between the free and restricted environments is slower than 10(3)/sec. The significance of these phenomena is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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