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- W2004233013 abstract "An analysis of the possible energy barriers to be overcome during processes of association and dissociation of intrinsic membrane proteins within a biological membrane is presented. The lack of necessary thermodynamic data proscribes accurate quantitative calculation. Nevertheless, by introducing a simple model, in which a putative common transition state is proposed for both processes, it becomes possible to predict qualitatively that the dynamic equilibrium between different aggregation states of membrane proteins might come about very slowly within the membrane (it may even be blocked under appropriate conditions). This is an inference that arises independently from recent experimental data (Swanson, M.S., Quintanilla, A.T. and Thomas, D.D. (1980) J. Biol. Chem. 255, 7494–7502, and Gutierrez-Merino, C. and Biltonen, R.L., unpublished data) involving cytochrome c and Ca2+-ATPase reconstituted systems, respectively. On the basis of this analysis there arises the possibility of unifying rationalization for the regulation of various membrane-mediated process such catalytic activity, transport processes, hormone responsiveness, and so forth, by physicochemical factors." @default.
- W2004233013 created "2016-06-24" @default.
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- W2004233013 date "1983-02-01" @default.
- W2004233013 modified "2023-09-28" @default.
- W2004233013 title "On the rate of association and dissociation processes of intrinsic membrane proteins" @default.
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- W2004233013 doi "https://doi.org/10.1016/0005-2736(83)90469-8" @default.
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