Strength of hydrogen bond network takes crucial roles in the dissociation process of inhibitors from the hiv-1 protease binding pocket

PLoS ONE

Volumn 6, Issue 4, 2011, Pages

  Li, Dechang ^a   Ji, Baohua ^a,b   Hwang, Keh Chih ^a   Huang, Yonggang ^c  

^a TSINGHUA UNIVERSITY   (China)

^b BEIJING INSTITUTE OF TECHNOLOGY   (China)

^c Northwestern University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AHA 001; ENZYME INHIBITOR; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; RITONAVIR; UNCLASSIFIED DRUG; XK 263; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE INHIBITOR; P16 PROTEASE, HUMAN IMMUNODEFICIENCY VIRUS 1;

ARTICLE; CONTROLLED STUDY; DISSOCIATION; DRUG BINDING SITE; ENZYME ACTIVE SITE; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR DYNAMICS; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; DRUG DESIGN; KINETICS; METHODOLOGY; PROTEIN BINDING; STATISTICAL MODEL; TIME;

HUMAN IMMUNODEFICIENCY VIRUS 1;

CATALYTIC DOMAIN; CHEMISTRY, PHARMACEUTICAL; COMPUTER SIMULATION; DRUG DESIGN; HIV PROTEASE; HIV PROTEASE INHIBITORS; HYDROGEN BONDING; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MODELS, STATISTICAL; MOLECULAR DYNAMICS SIMULATION; PROTEIN BINDING; TIME FACTORS;

EID: 79955786020     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019268     Document Type: Article

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