Title : Thermodynamics of lipid protein associations. Thermodynamics of helix formation in the association of high density apolipoprotein A-I (apoA-I) to dimyristoyl phosphatidylcholine.

Pub. Date : 1977 Aug 24

PMID : 19081






6 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Thermodynamics of helix formation in the association of high density apolipoprotein A-I (apoA-I) to dimyristoyl phosphatidylcholine. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
2 Thermodynamics of helix formation in the association of high density apolipoprotein A-I (apoA-I) to dimyristoyl phosphatidylcholine. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
3 At pH values of 7.4 and 3.1, apoA-I binds to dimyristoyl phosphatidylcholine (DMPC) to form complexes of similar composition (molar ratio of DMPC/apoA-I of 100) and helical content (67%). Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
4 At pH values of 7.4 and 3.1, apoA-I binds to dimyristoyl phosphatidylcholine (DMPC) to form complexes of similar composition (molar ratio of DMPC/apoA-I of 100) and helical content (67%). Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
5 At pH values of 7.4 and 3.1, apoA-I binds to dimyristoyl phosphatidylcholine (DMPC) to form complexes of similar composition (molar ratio of DMPC/apoA-I of 100) and helical content (67%). Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
6 At pH 3.1, the helical content of apoA-I is increased from 48 to 67% on binding to DMPC and the enthalpy of binding was -170 kcal/mol. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens