期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 101, 期 12, 页码 4071-4076出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0307804101
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Analytic estimates for the forces and free energy generated by bilayer deformation reveal a compelling and intuitive model for MscL channel gating analogous to the nucleation of a second phase. We argue that the competition between hydrophobic mismatch and tension results in a surprisingly rich story that can provide both a quantitative comparison with measurements of opening tension for MscL when reconstituted in bilayers of different thickness, and qualitative insights into the function of the MscL channel and other transmembrane proteins.
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