title: Membrane composition variation and underdamped mechanics near transmembrane proteins and coats.
abstract: We study the effect of transmembrane proteins on the shape, composition, and thermodynamic stability of the surrounding membrane. When the coupling between membrane composition and curvature is strong enough, the nearby membrane composition and shape both undergo a transition from overdamped to underdamped spatial variation, well before the membrane becomes unstable in the bulk. This transition is associated with a change in the sign of the thermodynamic energy and, hence, favors the early stages of coat assembly necessary for vesiculation (budding) and may suppress the activity of mechanosensitive membrane channels and transporters. Our results suggest an approach to obtain physical parameters of the membrane that are otherwise difficult to measure.
authors: Department of Physics, University of Warwick, Coventry CV4 7AL, United Kingdom.
authors: S Alex
authors: SA
authors: Rautu
authors: Department of Physics, University of Warwick, Coventry CV4 7AL, United Kingdom.
authors: George
authors: G
authors: Rowlands
authors: Department of Physics, University of Warwick, Coventry CV4 7AL, United Kingdom.|Centre for Complexity Science, University of Warwick, Coventry CV4 7AL, United Kingdom.
authors: Matthew S
authors: MS
authors: Turner
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008566:Membranes / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D013816:Thermodynamics
chemical_list: D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins