title: Protein folding mechanisms studied by pulsed oxidative labeling and mass spectrometry.
abstract: Deciphering the mechanisms of protein folding remains a considerable challenge. In this review we discuss the application of pulsed oxidative labeling for tracking protein structural changes in a time-resolved fashion. Exposure to a microsecond OH pulse at selected time points during folding induces the oxidation of solvent-accessible side chains, whereas buried residues are protected. Oxidative modifications can be detected by mass spectrometry. Folding is associated with dramatic accessibility changes, and therefore this method can provide detailed mechanistic insights. Solvent accessibility patterns are complementary to H/D exchange investigations, which report on the extent of hydrogen bonding. This review highlights the application of pulsed OH labeling to soluble proteins as well as membrane proteins.
authors.affiliation: Department of Chemistry, The University of Western Ontario, London, ON N6A 5B7, Canada. konerman@uwo.ca
authors.forename: Lars
authors.initials: L
authors.lastname: Konermann
authors.forename: Yan
authors.initials: Y
authors.lastname: Pan
authors.forename: Bradley B
authors.initials: BB
authors.lastname: Stocks
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry; D006860:Hydrogen Bonding; D007700:Kinetics; D013058:Mass Spectrometry / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry*; D015336:Molecular Probe Techniques; D015335:Molecular Probes / Q000737:chemistry; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017510:Protein Folding; D012995:Solubility; D012997:Solvents / Q000737:chemistry; D013997:Time Factors
chemical_list: D008565:Membrane Proteins; D015335:Molecular Probes; D012997:Solvents; D001436:Bacteriorhodopsins