Abstract
AbstractThermodynamic relationships have been derived to describe the change in the entropy (ΔS) of lipid vesicles in the presence of a protein in terms of experimental quantities, the concentration of protein (C), the temperature (tm), and the enthalpy (ΔH) of the main lipid phase transition. Knowledge of the change in ΔS 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 ΔH and tm with respect to C. In a special cae where tm remains inchanged and (ΔH) varies, the change in ΔS can be represented simply as (ΔHc − ΔHo)/Tm, where the subscripts c and o denote the presence and absence of a protein, respectively. Data for 1,2‐dimyristoyl phosphatidylcholone in the presence of lysozyme was used to illustrate a thermodynamic analysis.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
