Escherichia coli adenylate kinase dynamics: Comparison of elastic network model modes with mode-coupling 15N-NMR relaxation data

Proteins: Structure, Function and Genetics

Volumn 57, Issue 3, 2004, Pages 468-480

  Temiz, N Alpay ^a   Meirovitch, Eva ^a,b   Bahar, Ivet ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

^b BAR ILAN UNIVERSITY   (Israel)

Author keywords

Collective modes; Conformational changes; Gaussian network model; Slowly Relaxing Local Structure

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; ENZYME; LIGAND; MAGNESIUM ION;

ANISOTROPY; ARTICLE; CATALYSIS; ELASTICITY; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; INTERMETHOD COMPARISON; LIGAND BINDING; MODEL; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; MOTION; NITROGEN NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; TIME;

ADENYLATE KINASE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ELASTICITY; ESCHERICHIA COLI; KINETICS; LIGANDS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOVEMENT; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, TERTIARY; REPRODUCIBILITY OF RESULTS;

ESCHERICHIA COLI;

EID: 6344231648     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20226     Document Type: Article

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