NDLI: Bilayer-thickness-mediated interactions between integral membrane proteins.

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Bilayer-thickness-mediated interactions between integral membrane proteins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kahraman, Osman Koch, Peter D. Klug, William S. Haselwandter, Christoph A.
Description	Country affiliation: United States Author Affiliation: Kahraman O ( Department of Physics & Astronomy and Molecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, California 90089, USA.); Koch PD ( Department of Systems Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.); Klug WS ( Department of Mechanical and Aerospace Engineering, University of California, Los Angeles, California 90095, USA.); Haselwandter CA ( Department of Physics & Astronomy and Molecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, California 90089, USA.)
Abstract	Hydrophobic thickness mismatch between integral membrane proteins and the surrounding lipid bilayer can produce lipid bilayer thickness deformations. Experiment and theory have shown that protein-induced lipid bilayer thickness deformations can yield energetically favorable bilayer-mediated interactions between integral membrane proteins, and large-scale organization of integral membrane proteins into protein clusters in cell membranes. Within the continuum elasticity theory of membranes, the energy cost of protein-induced bilayer thickness deformations can be captured by considering compression and expansion of the bilayer hydrophobic core, membrane tension, and bilayer bending, resulting in biharmonic equilibrium equations describing the shape of lipid bilayers for a given set of bilayer-protein boundary conditions. Here we develop a combined analytic and numerical methodology for the solution of the equilibrium elastic equations associated with protein-induced lipid bilayer deformations. Our methodology allows accurate prediction of thickness-mediated protein interactions for arbitrary protein symmetries at arbitrary protein separations and relative orientations. We provide exact analytic solutions for cylindrical integral membrane proteins with constant and varying hydrophobic thickness, and develop perturbative analytic solutions for noncylindrical protein shapes. We complement these analytic solutions, and assess their accuracy, by developing both finite element and finite difference numerical solution schemes. We provide error estimates of our numerical solution schemes and systematically assess their convergence properties. Taken together, the work presented here puts into place an analytic and numerical framework which allows calculation of bilayer-mediated elastic interactions between integral membrane proteins for the complicated protein shapes suggested by structural biology and at the small protein separations most relevant for the crowded membrane environments provided by living cells.
File Format	HTM / HTML
ISSN	24700045
e-ISSN	24700053
Journal	Physical Review E
Volume Number	93
Language	English
Publisher	American Physical Society
Publisher Date	2016-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Statistical and Nonlinear Physics many-body systems Condensed Matter Physics
Content Type	Text
Resource Type	Article
Subject	Statistics and Probability Statistical and Nonlinear Physics Condensed Matter Physics

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