Conformer-specific characterization of nonnative protein states using hydrogen exchange and top-down mass spectrometry.

ABSTRACT: Characterization of structure and dynamics of nonnative protein states is important for understanding molecular mechanisms of processes as diverse as folding, binding, aggregation, and enzyme catalysis to name just a few; however, selectively probing local minima within rugged energy landscapes remains a problem. Mass spectrometry (MS) coupled with hydrogen/deuterium exchange (HDX) offers a unique advantage of being able to make a distinction among multiple protein conformers that coexist in solution; however, detailed structural interrogation of such states previously remained out of reach of HDX MS. In this work, we exploited the aforementioned unique feature of HDX MS in combination with the ability of MS to isolate narrow populations of protein ions to characterize individual protein c

SUBMITTER: Wang G 

PROVIDER: S-EPMC3864316 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature