title: Conformational Dynamics and Interactions of Membrane Proteins by Hydrogen/Deuterium Mass Spectrometry.
abstract: Hydrogen/deuterium exchange associated with mass spectrometry has been recently used to characterize the dynamics and the interactions of membrane proteins. Here we describe experimental workflow enabling localization of the regions involved in conformational changes or interactions.
authors.affiliation: Univ. Grenoble Alpes, IBS, Grenoble, France. eric.forest@ibs.fr.|CNRS, IBS, Grenoble, France. eric.forest@ibs.fr.|CEA, IBS, Grenoble, France. eric.forest@ibs.fr.|Institut de Biologie Structurale, CNRS (UMR 5075)/CEA/UGA, EPN Campus, 71 avenue des Martyrs, CS 10090, 38044, Grenoble Cedex 9, France. eric.forest@ibs.fr.
authors.forename: Eric
authors.initials: E
authors.lastname: Forest
authors.affiliation: BioCeV - Institute of Microbiology, Czech Academy of Sciences, Vestec, Czech Republic.|Faculty of Science, Charles University in Prague, Prague, Czech Republic.
authors.forename: Petr
authors.initials: P
authors.lastname: Man
mesh_terms: D001665:Binding Sites; D041961:Deuterium Exchange Measurement / Q000295:instrumentation* / Q000379:methods; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D008565:Membrane Proteins
keywords: Conformational change; Dynamics; Hydrogen/deuterium exchange; Interaction; Mass spectrometry; Membrane protein