Open AccessMembrane-induced interactions between curvature-generating protein domains: the role of area perturbation
Author(s) -
Nily Dan
Publication year - 2017
Publication title -
aims biophysics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.545
H-Index - 12
ISSN - 2377-9098
DOI - 10.3934/biophy.2017.1.107
Subject(s) - curvature , membrane , perturbation (astronomy) , bending , biophysics , moduli , bar (unit) , chemical physics , membrane protein , monotonic function , chemistry , materials science , crystallography , physics , geometry , mathematics , composite material , biology , mathematical analysis , biochemistry , quantum mechanics , meteorology
Membrane deformation by asymmetric crescent-shaped proteins such as BAR-domains is calculated, using a mean field model that accounts for both bending and area stretch deformations. The penalties associated with membrane bending and area perturbation lead to moderately long-ranged (order 10 nm), non-monotonic, membrane-induced interactions between proteins that may prevent the formation of closely packed aggregates. As a result, BAR-domain proteins may favor the formation of an ordered array with a specific separation between domains whose spacing is set by the ratio between the bending and area stretch moduli