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
Biochemistryjournal_title
Biochemistryauthors
Brophy PJ,Horváth LI,Marsh Ddoi
10.1021/bi00300a011subject
Has Abstractpub_date
1984-02-28 00:00:00pages
860-5issue
5eissn
0006-2960issn
1520-4995journal_volume
23pub_type
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