Year: 1996
Type: article
Abstract: We model membrane proteins as anisotropic objects characterized by symmetric-traceless tensors and determine the coupling between these order-parameters and membrane curvature. We consider the interactions between transmembrane proteins that respect up-down (reflection) symmetry of bilayer membranes and that have circular or non-circular cross-sectional areas in the tangent-plane of membranes. Using a field theoretic approach, we find non-entropic $1/R^{4}$ interactions between reflection-symmetry-breaking transmembrane proteins with circular cross-sectional area and entropic $1/R^{4}$ interactions between transmembrane proteins with circular cross-section that do not break up-down symmetry in agreement with previous calculations. We also find anisotropic $1/R^{4}$ interactions between reflection-symmetry-conserving transmembrane proteins with non-circular cross-section, anisotropic $1/R^{2}$ interactions between reflection-symmetry-breaking transmembrane proteins with non-circular cross-section, and non-entropic $1/R^{4}$ many-particle interactions among non-transmembrane proteins. For large $R$, these interactions might provide the dominant force inducing aggregation of the membrane proteins.
Source: Journal de Physique I
DOI: 10.1051/jp1:1996125
Authors: Jeong-Man Park, T. C. Lubensky
Institution: University of Pennsylvania
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W1966358634