title: Probing conformational changes in rhodopsin using hydrogen-deuterium exchange coupled to mass spectrometry.
abstract: Hydrogen-deuterium exchange coupled to mass spectrometry is a powerful tool to evaluate changes in protein conformation between two or more states. Here, we describe a complete methodology that can be used to assess conformational changes in rhodopsin accompanying its transition from the inactive to activated state upon light exposure. This approach may be employed to investigate the structure and conformational changes of various membrane proteins.
authors.affiliation: Department of Pharmacology, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH, 44106-4965, USA, txo54@case.edu.
authors.forename: Tivadar
authors.initials: T
authors.lastname: Orban
authors.forename: Yaroslav
authors.initials: Y
authors.lastname: Tsybovsky
mesh_terms: D003903:Deuterium / Q000737:chemistry*; D041961:Deuterium Exchange Measurement / Q000379:methods*; D006859:Hydrogen / Q000737:chemistry*; D013058:Mass Spectrometry; D012243:Rhodopsin / Q000737:chemistry*
chemical_list: D006859:Hydrogen; D012243:Rhodopsin; D003903:Deuterium