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 info rmation regarding correlated motions occurring on the microseconds to secon ds timescale. To expand the applicability of MS to these studies, a new alg orithm has been developed to interpret MS data for exchange occurring betwe en the EX2 and EX1 kinetic limits. Re-interpretation of MS data for ovomuco id third domain multiple unfolding or partial unfolding reactions limits re veals (C) 2000 Academic Press.