title: Conformation of cytochrome c studied by deuterium exchange-electrospray ionization mass spectrometry.
abstract: Deuterium exchange of bovine cytochrome c has been monitored by electrospray ionization mass spectrometry. Different charge-state distributions in the mass spectrum appear to represent different protein conformations, but rapid interconversion of the conformations can lead to a coincidence of the deuterium exchange rates. When interconversion is blocked, the conformation corresponding to higher m/z (lower charge) exchanges more slowly, indicating a tightly folded state. Furthermore, the data suggest that at least two conformations can have identical charge-state distributions, but have different exchange rates. Thus, neither charge-state distribution nor deuterium exchange rate alone is a sufficient indicator of protein conformation.
authors.affiliation: Glaxo Research Institute, Research Triangle Park, North Carolina 27709.
authors.forename: D S
authors.initials: DS
authors.lastname: Wagner
authors.forename: R J
authors.initials: RJ
authors.lastname: Anderegg
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003574:Cytochrome c Group / Q000737:chemistry*; D003903:Deuterium; D007477:Ions; D013058:Mass Spectrometry / Q000379:methods*; D011487:Protein Conformation
chemical_list: D003574:Cytochrome c Group; D007477:Ions; D003903:Deuterium