pH-REMD simulations indicate that the catalytic aspartates of HIV-1 protease exist primarily in a monoprotonated state

Journal of Physical Chemistry B

Volumn 118, Issue 44, 2014, Pages 12577-12585

  McGee, T Dwight ^a   Edwards, Jesse ^b   Roitberg, Adrian E ^a  

^a University of Florida   (United States)

^b FLORIDA A AND M UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATES; HIV-1 PROTEASE;

ASPARTIC ACID; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE INHIBITOR; P16 PROTEASE, HUMAN IMMUNODEFICIENCY VIRUS 1; PROTON;

BIOCATALYSIS; CHEMISTRY; DRUG DESIGN; ENZYME ACTIVE SITE; KINETICS; MOLECULAR DYNAMICS; PH; THERMODYNAMICS;

ASPARTIC ACID; BIOCATALYSIS; CATALYTIC DOMAIN; DRUG DESIGN; HIV PROTEASE; HIV PROTEASE INHIBITORS; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR DYNAMICS SIMULATION; PROTONS; THERMODYNAMICS;

EID: 84908612291     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp504011c     Document Type: Article

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