title: Time-resolved pulsed hydrogen/deuterium exchange mass spectrometry probes gaseous proteins structural kinetics.
abstract: A pulsed hydrogen/deuterium exchange (HDX) method has been developed for rapid monitoring of the exchange kinetics of protein ions with D2O a few milliseconds after electrospray ionization (ESI). The stepwise gradual evolution of HDX of multiply charged protein ions was monitored using the pulsed HDX mass spectrometry technique. Upon introducing a very short pulse of D2O (in the μs to ms time scale) into the linear ion trap (LIT) of a time-of-flight (TOF) mass spectrometer, bimodal distributions were detected for the ions of cytochrome c and ubiquitin. Mechanistic details of HDX reactions for ubiquitin and cytochrome c in the gas phase were uncovered and the structural transitions were followed by analyzing the kinetics of HDX.
authors.affiliation: Department of Chemistry, University of British Columbia (UBC), 2036 Mail Mall, Vancouver, BC, V6T 1Z1, Canada, k.n.rajabi@leeds.ac.uk.
authors.forename: Khadijeh
authors.initials: K
authors.lastname: Rajabi
mesh_terms: D041961:Deuterium Exchange Measurement / Q000379:methods*; D007700:Kinetics; D013058:Mass Spectrometry / Q000379:methods*; D011506:Proteins / Q000032:analysis* / Q000737:chemistry
chemical_list: D011506:Proteins