Stoichiometry and specificity of lipid-protein interaction with myelin proteolipid protein studied by spin-label electron spin resonance.

Abstract:

:The interaction of spin-labeled lipids with the myelin proteolipid apoprotein in complexes with dimyristoylphosphatidylcholine of varying lipid/protein ratios has been studied with electron spin resonance spectroscopy. A first shell of approximately 10 lipids per 25 000-dalton protein is found to be motionally restricted by the protein interface. This stoichiometry is consistent with a hexameric arrangement of the protein in the membrane. A selectivity of the various spin-labeled lipids for the motionally restricted component at the protein interface is found in the order stearic acid greater than phosphatidic acid greater than cardiolipin approximately greater than phosphatidylserine greater than phosphatidylglycerol approximately equal to phosphatidylcholine greater than phosphatidylethanolamine greater than androstanol approximately greater than cholestane.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Brophy PJ,Horváth LI,Marsh D

doi

10.1021/bi00300a011

subject

Has Abstract

pub_date

1984-02-28 00:00:00

pages

860-5

issue

5

eissn

0006-2960

issn

1520-4995

journal_volume

23

pub_type

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