Modeling of transition state by molecular dynamics. Prediction of catalytic efficiency of the mutants of mandelate racemase

Journal of Biomolecular Structure and Dynamics

Volumn 28, Issue 6, 2011, Pages 871-879

  Zhuohang, Mei ^a   Ji, Liu ^a   Hongwei, Yu ^a  

^a ZHEJIANG UNIVERSITY   (China)

Author keywords

Catalytic efficiency; Free energy; Mandelate racemase; Molecular dynamic; Rational design

Indexed keywords

MANDELATE RACEMASE;

ANALYTICAL ERROR; ARTICLE; BINDING SITE; CHEMICAL INTERACTION; COMPUTER PROGRAM; CONTROLLED STUDY; ENANTIOMER; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; MATHEMATICAL ANALYSIS; MATHEMATICAL MODEL; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; PHASE TRANSITION; PREDICTION; PRIORITY JOURNAL;

BINDING SITES; BIOCATALYSIS; CATALYTIC DOMAIN; ENERGY METABOLISM; MANDELIC ACIDS; MOLECULAR DYNAMICS SIMULATION; MUTANT PROTEINS; PROTEIN BINDING; RACEMASES AND EPIMERASES; THERMODYNAMICS;

EID: 79958708798     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2011.10508614     Document Type: Article

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