Title : Evidence for protein-associated lipids from deuterium nuclear magnetic resonance studies of rhodopsin-dimyristoylphosphatidylcholine recombinants.

Pub. Date : 1982 Mar 25

PMID : 7061462






3 Functional Relationships(s)
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1 Evidence for protein-associated lipids from deuterium nuclear magnetic resonance studies of rhodopsin-dimyristoylphosphatidylcholine recombinants. Dimyristoylphosphatidylcholine rhodopsin Homo sapiens
2 The technique of deuterium magnetic resonance was used to study the orientational order of the perdeuterated acyl chains of dimyristoylphosphatidylcholine (DMPC-d54) reconstituted with rhodopsin between 0 and 23 degrees C. This range includes the gel to liquid crystalline phase transition of DMPC-d54 at 20 degrees C. Molar lipid/protein (L/P) ratios of L/P = infinity, 150, 50, 30, and 12 were investigated. Dimyristoylphosphatidylcholine rhodopsin Homo sapiens
3 The technique of deuterium magnetic resonance was used to study the orientational order of the perdeuterated acyl chains of dimyristoylphosphatidylcholine (DMPC-d54) reconstituted with rhodopsin between 0 and 23 degrees C. This range includes the gel to liquid crystalline phase transition of DMPC-d54 at 20 degrees C. Molar lipid/protein (L/P) ratios of L/P = infinity, 150, 50, 30, and 12 were investigated. Dimyristoylphosphatidylcholine rhodopsin Homo sapiens