Minimum free energy path of ligand-induced transition in Adenylate kinase

PLoS Computational Biology

Volumn 8, Issue 6, 2012, Pages

  Matsunaga, Yasuhiro ^a   Fujisaki, Hiroshi ^a,b   Terada, Tohru ^a,c   Furuta, Tadaomi ^a,d   Moritsugu, Kei ^a   Kidera, Akinori ^a,e  

^a RIKEN   (Japan)

^b NIPPON MEDICAL SCHOOL   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^e YOKOHAMA CITY UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; ENZYMES; ESCHERICHIA COLI; FREE ENERGY; MOLECULAR DYNAMICS;

ACCEPTANCE RATIO METHOD; ADENYLATE KINASE; BENNETT ACCEPTANCE RATIO; BINDING DOMAIN; CONFORMATIONAL TRANSITIONS; ENERGY PATHS; HIGH DIMENSIONAL SPACES; MINIMUM FREE ENERGIES; MULTI-STATE; STRING METHODS;

LIGANDS;

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; BACTERIAL ENZYME; ESCHERICHIA COLI PROTEIN; LIGAND;

ALGORITHM; ARTICLE; BINDING SITE; BIOCHEMICAL COMPOSITION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STABILITY; HYDROGEN BOND; LIGAND BINDING; MATHEMATICAL ANALYSIS; MATHEMATICAL MODEL; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; SIGNAL TRANSDUCTION; BIOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; ENTROPY; ENZYMOLOGY; ESCHERICHIA COLI; METABOLISM; PROTEIN CONFORMATION;

ESCHERICHIA COLI;

ADENOSINE MONOPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; ENTROPY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LIGANDS; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION;

EID: 84864035485     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002555     Document Type: Article

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