Role of Enzyme Flexibility in Ligand Access and Egress to Active Site: Bias-Exchange Metadynamics Study of 1,3,7-Trimethyluric Acid in Cytochrome P450 3A4

Journal of Chemical Theory and Computation

Volumn 12, Issue 4, 2016, Pages 2101-2109

  Paloncýová, Markéta ^a   Navrátilová, Veronika ^a   Berka, Karel ^a   Laio, Alessandro ^b   Otyepka, Michal ^a  

^a PALACKÝ UNIVERSITY   (Czech Republic)

^b SISSA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

1,3,7-TRIMETHYLURIC ACID; CYP3A4 PROTEIN, HUMAN; CYTOCHROME P450 3A; LIPID BILAYER; URIC ACID;

ANALOGS AND DERIVATIVES; CHEMISTRY; ENZYME ACTIVE SITE; HUMAN; LIPID BILAYER; METABOLISM; MOLECULAR DYNAMICS; PROTEIN CONFORMATION; THERMODYNAMICS;

CATALYTIC DOMAIN; CYTOCHROME P-450 CYP3A; HUMANS; LIPID BILAYERS; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; THERMODYNAMICS; URIC ACID;

EID: 84964426734     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/acs.jctc.6b00075     Document Type: Article

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