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* Department of Physics and Department of Chemistry & Biochemistry, University of California, Santa Barbara, California;
Department of Chemistry & Biochemistry and California Nanosystems Institute, University of California, Los Angeles, California; and
Materials Research Laboratory, and Departments of Physics and Materials, Biomolecular Science & Engineering, University of California, Santa Barbara, California
Correspondence: Address reprint requests and inquiries to Alex J. Levine, E-mail: alevine{at}chem.ucla.edu.
Recent experiments (Gambin, Y., R. Lopez-Esparza, M. Reffay, E. Sierecki, N. S. Gov, M. Genest, R. S. Hodes, and W. Urbach. 2006. Proc. Natl. Acad. Sci. USA. 103:2098–2102) have called into question the applicability of the Saffman-Delbrück diffusivity for proteins embedded in the lipid bilayers. We present a simple argument to account for this observation that should be generically valid for a large class of transmembrane and membrane bound proteins. Whenever the protein-lipid interactions locally deform the membrane, that deformation generates new hydrodynamic stresses on the protein-membrane complex leading to a suppression of its mobility. We show that this suppression depends on the protein size in a manner consistent with the work of Gambin et al.
This article has been cited by other articles:
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G. Guigas and M. Weiss Influence of Hydrophobic Mismatching on Membrane Protein Diffusion Biophys. J., August 1, 2008; 95(3): L25 - L27. [Abstract] [Full Text] [PDF] |
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