Statistical Mechanics of Membrane Protein Conformation: A Homopolymer Model
Open Access
- 22 June 1998
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 80 (25) , 5687-5690
- https://doi.org/10.1103/physrevlett.80.5687
Abstract
The conformation and the phase diagram of a membrane protein are investigated via grand canonical ensemble approach using a homopolymer model. We discuss the nature and pathways of -helix integration into the membrane that result depending upon membrane permeability and polymer adsorptivity. For a membrane with the permeability larger than a critical value, the integration becomes the second order transition that occurs at the same temperature as that of the adsorption transition. For a nonadsorbing membrane, the integration is of the first order due to the aggregation of helices.
Keywords
All Related Versions
This publication has 24 references indexed in Scilit:
- Pathways for protein folding: is a new view needed?Current Opinion in Structural Biology, 1998
- Chain Length Scaling of Protein Folding TimePhysical Review Letters, 1996
- Navigating the Folding RoutesScience, 1995
- Random hydrophilic-hydrophobic copolymersJournal de Physique II, 1994
- Adsorption of polymer chains at surfaces: Scaling and Monte Carlo analysesThe Journal of Chemical Physics, 1982
- Some problems of the statistical physics of polymer chains with volume interactionReviews of Modern Physics, 1978
- Adsorption of a macromolecule to a charged surfaceJournal of Physics A: General Physics, 1977
- Three-dimensional model of purple membrane obtained by electron microscopyNature, 1975
- PROTEIN CONFORMATION IN CELL MEMBRANE PREPARATIONS AS STUDIED BY OPTICAL ROTATORY DISPERSION AND CIRCULAR DICHROISMProceedings of the National Academy of Sciences, 1966
- Protein conformations in cellular membranes.Proceedings of the National Academy of Sciences, 1966