Domain motions and the open-to-closed conformational transition of an enzyme: A normal mode analysis of S-adenosyl-L-homocysteine hydrolase

Biochemistry

Volumn 44, Issue 19, 2005, Pages 7228-7239

  Wang, Mengmeng ^a   Borchardt, Ronald T ^a   Schowen, Richard L ^a   Kuczera, Krzysztof ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; CONFORMATIONS; ENZYME INHIBITION; FLUORESCENCE; POLARIZATION; PROTEINS; REACTION KINETICS;

CONFORMATIONAL TRANSITION; DEPOLARIZATION; DOMAIN MOTIONS; FREQUENCY VIBRATION; TETRAMERIC ENZYMES;

ENZYMES;

ADENOSYLHOMOCYSTEINASE;

ARTICLE; CALCULATION; DEPOLARIZATION; ENZYME MECHANISM; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN CONFORMATION;

ADENINE; ADENOSINE; ADENOSYLHOMOCYSTEINASE; ANIMALS; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME INHIBITORS; HUMANS; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RATS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 18544386701     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047524m     Document Type: Article

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