Ontology highlight
ABSTRACT:
SUBMITTER: Long D
PROVIDER: S-EPMC4066525 | biostudies-literature | 2014 Jun
REPOSITORIES: biostudies-literature
Long Dong D Bouvignies Guillaume G Kay Lewis E LE
Proceedings of the National Academy of Sciences of the United States of America 20140602 24
Hydrogen exchange rates have become a valuable probe for studying the relationship between dynamics and structure and for dissecting the mechanism by which proteins fold to their native conformation. Typically measured rates correspond to averages over all protein states from which hydrogen exchange can occur. Here we describe a new NMR experiment based on chemical exchange saturation transfer that provides an avenue for obtaining uncontaminated, per-residue amide hydrogen exchange rates for int ...[more]