期刊
PLOS COMPUTATIONAL BIOLOGY
卷 3, 期 5, 页码 803-812出版社
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pcbi.0030081
关键词
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资金
- NIGMS NIH HHS [K25 GM075000, A1K25 GM75000] Funding Source: Medline
- NIH HHS [DP1 OD000217, DP1 OD000217-03] Funding Source: Medline
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 similar to 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.
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