Correlated motions in native proteins from MS analysis of NH exchange: evidence for a manifold of unfolding reactions in ovomucoid third domain.
Native-state amide hydrogen exchange monitored by NMR spectroscopy and mass spectrometry (MS) has the potential to provide detailed residue-level information regarding correlated motions occurring on the microseconds to seconds timescale. To expand the applicability of MS to these studies, a new algorithm has been developed to interpret MS data for exchange occurring between the EX2 and EX1 kinetic limits. Re-interpretation of MS data for ovomucoid third domain reveals multiple unfolding or partial unfolding reactions.
Arrington
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CB
Department of Biochemistry, University of Iowa, Iowa City, IA, USA.
Robertson
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AD
D000465:Algorithms; D000588:Amines / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D003198:Computer Simulation; D006859:Hydrogen / Q000378:metabolism; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013058:Mass Spectrometry / Q000379:methods; D009038:Motion; D010059:Ovomucin / Q000737:chemistry* / Q000378:metabolism*; D011336:Probability; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D014422:Turkeys
D000588:Amines; D010059:Ovomucin; D006859:Hydrogen