cooperative gating and spatial organization of membrane proteins through elastic interactions合作控制和空间组织通过弹性膜蛋白的相互作用.pdfVIP
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cooperative gating and spatial organization of membrane proteins through elastic interactions合作控制和空间组织通过弹性膜蛋白的相互作用
Cooperative Gating and Spatial Organization of
Membrane Proteins through Elastic Interactions
1 2 3 1,4*
Tristan Ursell , Kerwyn Casey Huang , Eric Peterson , Rob Phillips
1 Department of Applied Physics, California Institute of Technology, Pasadena, California, United States of America, 2 Department of Molecular Biology, Princeton University,
Princeton, New Jersey, United States of America, 3 Department of Physics, California Institute of Technology, Pasadena, California, United States of America, 4 Kavli
Nanoscience Institute, Pasadena, California, United States of America
Biological membranes are elastic media in which the presence of a transmembrane protein leads to local bilayer
deformation. The energetics of deformation allow two membrane proteins in close proximity to influence each other’s
equilibrium conformation via their local deformations, and spatially organize the proteins based on their geometry. We
use the mechanosensitive channel of large conductance (MscL) as a case study to examine the implications of bilayer-
mediated elastic interactions on protein conformational statistics and clustering. The deformations around MscL cost
energy on the order of 10 kBT and extend ;3 nm from the protein edge, as such elastic forces induce cooperative
gating, and we propose experiments to measure these effects. Additionally, since elastic interactions are coupled to
protein conformation, we find that conformational changes can severely alter the average separation between two
proteins. This has important implications for how conformational changes organize membrane proteins into functional
groups within membranes.
Citation: Ursell T, Huang KC, Peterson E, Phillips R (2007) Cooperative gating and spatial organization of membrane proteins through elastic interactions. PLoS Comput Biol
3(5): e81. doi:10
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