Wiggins, Paul and Phillips, Rob (2004) Analytic models for mechanotransduction: gating a mechanosensitive channel. Proceedings of the National Academy of Sciences of the United States of America, 101 (12). pp. 4071-4076. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:WIGpnas04
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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.
|Additional Information:||Copyright © 2004 by the National Academy of Sciences. Edited by Douglas C. Rees, California Institute of Technology, Pasadena, CA, and approved January 22, 2004 (received for review November 24, 2003). Published online before print March 15, 2004, 10.1073/pnas.0307804101 We thank Doug Rees, Tom Powers, Jane Kondev, Klaus Schulten, Evan Evans, Sergei Sukharev, Eduardo Perozo, Olaf Andersen, Sylvio May, Ben Freund, Mandar Inamdar, and an anonymous referee for useful discussions, suggestions, and corrections. This work was supported by the Keck Foundation, National Science Foundation Grant CMS-0301657, and the National Science Foundation-funded Center for Integrative Multiscale Modeling and Simulation. P.W. received support through a National Science Foundation fellowship. This paper was submitted directly (Track II) to the PNAS office.|
|Subject Keywords:||ION-CHANNEL, MSCL, PROTEINS, TRANSDUCTION, MECHANISM, MEMBRANE, TENSION, RESIDUE, ENERGY|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||12 Jan 2006|
|Last Modified:||14 Nov 2014 19:18|
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