Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: A model for changes in dynamics upon target binding

Journal of Molecular Biology

Volumn 322, Issue 1, 2002, Pages 137-152

  Åkerud, Tomas ^a,b   Thulin, Eva ^a   Van Etten, Robert L ^c   Akke, Mikael ^a  

^a LUND UNIVERSITY   (Sweden)

^b BIOVITRUM AB   (Sweden)

^c PURDUE UNIVERSITY   (United States)

Author keywords

Conformational exchange; Dimerization; Enzyme dynamics; Order parameters; Rotational diffusion tensor

Indexed keywords

DIMER; MONOMER; NITROGEN 15; PHOSPHATE; PROTEIN TYROSINE PHOSPHATASE; TYROSINE;

ACCURACY; ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL BOND; CHEMICAL INTERACTION; CHEMICAL MODEL; CONCENTRATION (PARAMETERS); CONFORMATION; CORRELATION ANALYSIS; CRYSTAL STRUCTURE; DIMERIZATION; DISSOCIATION CONSTANT; ENZYME ANALYSIS; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; MUTANT; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN TARGETING; TIME;

EID: 0036967268     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00714-3     Document Type: Article

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