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NMR Relaxation Dispersion
Author(s) -
Loria Patrick
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.240.2
Subject(s) - microsecond , dispersion (optics) , active site , relaxation (psychology) , catalysis , chemistry , millisecond , chemical physics , protein tyrosine phosphatase , substrate (aquarium) , loop (graph theory) , tyrosine , biophysics , physics , biochemistry , biology , optics , ecology , mathematics , combinatorics , astronomy , neuroscience
NMR relaxation dispersion experiments are used to characterize millisecond and microsecond motions and the role of these motions in regulation of protein tyrosine phosphatases (PTPs) In a pair of mechanistically indistinguishable PTPs with catalytic rates that vary by 50‐fold these experiments indicate that catalytic activity is regulated by the rate of active site loop closure. Furthermore, it is observed that small molecule binding distant from the active site loop alters the kinetic rates of substrate catalysis as well as the dynamics of loop closure.