Volume 116, Number 2, October 2016
|Number of page(s)||7|
|Section||Interdisciplinary Physics and Related Areas of Science and Technology|
|Published online||28 November 2016|
Thermodynamic competition between membrane protein oligomeric states
Department of Physics & Astronomy and Molecular and Computational Biology Program, Department of Biological Sciences, University of Southern California - Los Angeles, CA 90089, USA
Received: 25 August 2016
Accepted: 8 November 2016
Self-assembly of protein monomers into distinct membrane protein oligomers provides a general mechanism for diversity in the molecular architectures, and resulting biological functions, of membrane proteins. We develop a general physical framework describing the thermodynamic competition between different oligomeric states of membrane proteins. Using the mechanosensitive channel of large conductance as a model system, we show how the dominant oligomeric states of membrane proteins emerge from the interplay of protein concentration in the cell membrane, protein-induced lipid bilayer deformations, and direct monomer-monomer interactions. Our results suggest general physical mechanisms and principles underlying regulation of protein function via control of membrane protein oligomeric state.
PACS: 87.16.D- – Membranes, bilayers, and vesicles / 87.16.Vy – Ion channels / 87.15.kt – Protein-membrane interactions
© EPLA, 2016
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