Back to Search
Start Over
Thermodynamics of membrane partitioning for a series of n-alcohols determined by titration calorimetry: role of hydrophobic effects
- Source :
- Biochemistry. Feb 24, 1998, Vol. 37 Issue 8, p2430, 11 p.
- Publication Year :
- 1998
-
Abstract
- The heat capacity change, partition coefficients and enthalpy for the partitioning of a series of n-alcohols were measured using titration calorimetry to understand the thermodynamics and determine the function of the hydrophobic effects in the partitioning of small amphiphilic molecules into lipib bilayers. The data were then compared with those of a model compound for partitioning into bulk hydrocarbon solvents. The results revealed that the thermodynamic state was dependent on dissolved solutes, temperature and lipid composition.
Details
- ISSN :
- 00062960
- Volume :
- 37
- Issue :
- 8
- Database :
- Gale General OneFile
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.20753190