Bilayer Thickness and Membrane Protein Function: An Energetic Perspective Export

@article{citeulike:1780051, abstract = {Abstract The lipid bilayer component of biological membranes is important for the distribution, organization, and function of bilayer-spanning proteins. This regulation is due to both specific lipid-protein interactions and general bilayer-protein interactions, which modulate the energetics and kinetics of protein conformational transitions, as well as the protein distribution between different membrane compartments. The bilayer regulation of membrane protein function arises from the hydrophobic coupling between the protein's hydrophobic domains and the bilayer hydrophobic core, which causes protein conformational changes that involve the protein/bilayer boundary to perturb the adjacent bilayer. Such bilayer perturbations, or deformations, incur an energetic cost, which for a given conformational change varies as a function of the bilayer material properties (bilayer thickness, intrinsic lipid curvature, and the elastic compression and bending moduli). Protein function therefore is regulated by changes in bilayer material properties, which determine the free-energy changes caused by the protein-induced bilayer deformation. The lipid bilayer thus becomes an allosteric regulator of membrane function.}, address = {Department of Physiology and Biophysics, Weill Medical College of Cornell University, New York, New York 10021, USA. sparre@med.cornell.edu}, author = {Andersen, Olaf S. and Koeppe, Roger E.}, citeulike-article-id = {1780051}, citeulike-linkout-0 = {http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biophys.36.040306.132643}, citeulike-linkout-1 = {http://dx.doi.org/10.1146/annurev.biophys.36.040306.132643}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/17263662}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=17263662}, doi = {10.1146/annurev.biophys.36.040306.132643}, issn = {1056-8700}, journal = {Annual Review of Biophysics and Biomolecular Structure}, keywords = {biological, biology, cell, essay, function, membrane, protein}, number = {1}, pages = {107--130}, posted-at = {2009-10-30 22:42:45}, priority = {5}, title = {Bilayer Thickness and Membrane Protein Function: An Energetic Perspective}, url = {http://dx.doi.org/10.1146/annurev.biophys.36.040306.132643}, volume = {36}, year = {2007} }

TY - JOUR ID - citeulike:1780051 L3 - citeulike-article-id:1780051 N2 - Abstract The lipid bilayer component of biological membranes is important for the distribution, organization, and function of bilayer-spanning proteins. This regulation is due to both specific lipid-protein interactions and general bilayer-protein interactions, which modulate the energetics and kinetics of protein conformational transitions, as well as the protein distribution between different membrane compartments. The bilayer regulation of membrane protein function arises from the hydrophobic coupling between the protein's hydrophobic domains and the bilayer hydrophobic core, which causes protein conformational changes that involve the protein/bilayer boundary to perturb the adjacent bilayer. Such bilayer perturbations, or deformations, incur an energetic cost, which for a given conformational change varies as a function of the bilayer material properties (bilayer thickness, intrinsic lipid curvature, and the elastic compression and bending moduli). Protein function therefore is regulated by changes in bilayer material properties, which determine the free-energy changes caused by the protein-induced bilayer deformation. The lipid bilayer thus becomes an allosteric regulator of membrane function. IS - 1 JF - Annual Review of Biophysics and Biomolecular Structure SN - 1056-8700 AD - Department of Physiology and Biophysics, Weill Medical College of Cornell University, New York, New York 10021, USA. sparre@med.cornell.edu EP - 130 TI - Bilayer Thickness and Membrane Protein Function: An Energetic Perspective VL - 36 SP - 107 KW - biological KW - biology KW - cell KW - essay KW - function KW - membrane KW - protein AU - Andersen, Olaf AU - Koeppe, Roger PY - 2007/// UR - http://dx.doi.org/10.1146/annurev.biophys.36.040306.132643 ER -