title: Hydrogen bond dynamics in membrane protein function.
abstract: Changes in inter-helical hydrogen bonding are associated with the conformational dynamics of membrane proteins. The function of the protein depends on the surrounding lipid membrane. Here we review through specific examples how dynamical hydrogen bonds can ensure an elegant and efficient mechanism of long-distance intra-protein and protein-lipid coupling, contributing to the stability of discrete protein conformational substates and to rapid propagation of structural perturbations. This article is part of a Special Issue entitled: Protein Folding in Membranes.
authors.affiliation: Theoretical Molecular Biophysics, Freie Universität Berlin, Department of Physics, Arnimallee 14, 14195 Berlin, Germany. nbondar@zedat.fu-berlin.de
authors.forename: Ana-Nicoleta
authors.initials: AN
authors.lastname: Bondar
authors.forename: Stephen H
authors.initials: SH
authors.lastname: White
mesh_terms: D006860:Hydrogen Bonding; D008051:Lipid Bilayers / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D017433:Protein Structure, Secondary
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins