Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis.

摘要: Proteins that undergo cooperative unfolding events display EX1 kinetic signatures in hydrogen exchange mass spectra. The hallmark bimodal isotope pattern observed for kinetics is distinct from the binomial uncorrelated (EX2), normal regime folded proteins. Detection and characterization of simple when unit large enough isotopic envelopes are resolved m/z scale but become complicated cases where small or there a mixture EX2 kinetics. Here we describe data interpretation method involving peak width analysis makes rapid. theoretical basis effects each have on described. Modeling widening empirical proteins peptides containing purely showed amount attributable to stochastic forward- back typical experiment can be quantified. with both obvious less were analyzed method. Such analyses provide half-life event relative number residues involved. Automated was performed custom Excel macros DEX software package. Peak robust, capable automation, provides quick key information contained events.