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Statistical Mechanics of Membrane Protein Conformation: A Homopolymer Model

1998/06/22 by Pyeong Jun Park, W. Sung · 17 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Physics and Astronomy · #Chemistry #Classical mechanics #Force Microscopy Techniques and Applications #Lipid Membrane Structure and Behavior #Materials science #Membrane #Molecular dynamics #Molecular mechanics #Physics #Protein Structure and Dynamics #Quantum mechanics #Statistical mechanics #Statistical physics #cond-mat.soft #q-bio

paper · pdf · doi:10.1103/physrevlett.80.5687

published in Physical Review Letters 80(25), 5687-5690 (American Physical Society) · RevTeX with 5 postscript figures

openalex publication_date 1998/06/22 · arxiv created 1998/07/01 · arxiv updated 2009/11/30 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05

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 \ensuremathα-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 \ensuremathα helices.

Citations