Conformational flexibility of the catalytic Asp dyad in HIV-1 protease: An ab initio study on the free enzyme

Proteins: Structure, Function and Genetics

Volumn 39, Issue 1, 2000, Pages 26-36

  Piana, Stefano ^a   Carloni, Paolo ^a,b,c  

^a INFM   (Italy)

^b INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Italy)

^c SISSA   (Italy)

Author keywords

Density functional theory; Human immunodeficiency virus type 1; Low barrier hydrogen bond; Molecular dynamics; Protease; Protonation state

Indexed keywords

ASPARTIC ACID; GLYCINE; PROTEINASE; THREONINE; VIRUS ENZYME;

ACQUIRED IMMUNE DEFICIENCY SYNDROME; ARTICLE; DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STABILITY; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS;

ASPARTIC ACID; CATALYTIC DOMAIN; COMPUTER SIMULATION; HIV PROTEASE; HUMANS; LIGANDS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; QUANTUM THEORY;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0033998647     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000401)39:1<26::AID-PROT3>3.0.CO;2-N     Document Type: Article

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