Thermodynamic examination of the ordering of lipid hydrocarbon chains in the presence of protein

✍ Scribed by Chang-Hwei Chen; Deborah Guard-Friar

• Publisher: Wiley (John Wiley & Sons)
• Year: 1985
• Tongue: English
• Weight: 454 KB
• Volume: 24
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360240403

✦ Synopsis

Thermodynamic relationships have been derived to describe the change in the entropy (AS) of lipid vesicles in the presence of a protein in terms of experimental quantities, the concentration of protein (0, the temperature (t,), and the enthalpy (AH) of the main lipid phase transition. Knowledge of the change in A S can provide an insight into the effect of a protein on the ordering of the lipid hydrocarbon chains. For a general case, evaluation of the entropy change requires information on the changes of AH and t,,, with respect to C. In a special case where t, remains unchanged and AHvaries, the change in A S can be represented simply as (AH, -AHJT,,,, where the subscripts c and o denote the presence and absence of a protein, respectively. Data for 1,2dimyristoyl phosphatidylcholine in the presence of lysozyme was used to illustrate a thermodynamic analysis.

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