Deuterium magnetic resonance studies of the interaction of lipids with membrane proteins.
AUTOR(ES)
Dahlquist, F W
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=431752Documentos Relacionados
- Deuterium Magnetic Resonance Studies of Senescence-Related Changes in the Physical Properties of Rose Petal Membrane Lipids.
- Nuclear magnetic resonance studies of proteins. I. Conformational variance among members of the chymotrypsinogen family.
- Deuterium nuclear magnetic resonance investigation of the effects of proteins and polypeptides on hydrocarbon chain order in model membrane systems
- 23Na NUCLEAR MAGNETIC RESONANCE RELAXATION STUDIES OF SODIUM ION INTERACTION WITH SOLUBLE RNA*
- Electron spin resonance studies on interaction of complement proteins with erythrocyte membranes.
