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Directional interactions and cooperativity between mechanosensitive membrane proteins

2012/09/30 by Christoph A. Haselwandter, Rob Phillips
Biochemistry, Genetics and Molecular Biology · Medicine · Physics and Astronomy · #Erythrocyte Function and Pathophysiology #Force Microscopy Techniques and Applications #Function (biology) #Ion channel #Lipid Membrane Structure and Behavior #Mechanosensitive channels #Membrane #Membrane biophysics #Membrane protein #Peripheral membrane protein #Protein–lipid interaction #Protein–protein interaction #cond-mat.soft #physics.bio-ph #q-bio.BM #q-bio.SC

paper · pdf · doi:10.1209/0295-5075/101/68002

published as EPL 101, 68002 (2013)

openalex publication_date 2013/03/01 · arxiv created 2013/05/24 · arxiv updated 2013/05/27 · openalex created_date 2016/06/24 · openalex updated_date 2026/08/06

Abstract

While modern structural biology has provided us with a rich and diverse picture of membrane proteins, the biological function of membrane proteins is often influenced by the mechanical properties of the surrounding lipid bilayer. Here we explore the relation between the shape of membrane proteins and the cooperative function of membrane proteins induced by membrane-mediated elastic interactions. For the experimental model system of mechanosensitive ion channels we find that the sign and strength of elastic interactions depend on the protein shape, yielding distinct cooperative gating curves for distinct protein orientations. Our approach predicts how directional elastic interactions affect the molecular structure, organization, and biological function of proteins in crowded membranes.

Citations