Title : Thermodynamics of the binding of human apolipoprotein A-I to dimyristoylphosphatidylglycerol.

Pub. Date : 1990 Dec 5

PMID : 2123484






4 Functional Relationships(s)
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Protein Name
Organism
1 Thermodynamics of the binding of human apolipoprotein A-I to dimyristoylphosphatidylglycerol. dimyristoylphosphatidylglycerol apolipoprotein A1 Homo sapiens
2 The interaction of human serum apolipoprotein A-I with dimyristoylphosphatidylglycerol was analyzed by isothermal titration calorimetry. dimyristoylphosphatidylglycerol apolipoprotein A1 Homo sapiens
3 Binding of the apolipoprotein A-I to large unilamellar vesicles of dimyristoylphosphatidylglycerol, a negatively charged phospholipid, is characterized by thermodynamic parameters which are invariant over the 30-40 degrees C temperature range. dimyristoylphosphatidylglycerol apolipoprotein A1 Homo sapiens
4 The binding isotherms for the high affinity binding of the apolipoprotein A-I to large unilammelar vesicles of dimyristoylphosphatidylglycerol, over the temperature range 30-40 degrees C, gave an enthalpy change of 1.43 +/- 0.07 kcal/mol of protein and a free energy change of -5.91 +/- 0.04 kcal/mol of protein for the binding of the protein to a cluster of 25 +/- 2 lipid molecules. dimyristoylphosphatidylglycerol apolipoprotein A1 Homo sapiens