Subtype polymorphisms among HIV-1 protease variants confer altered flap conformations and flexibility

Journal of the American Chemical Society

Volumn 131, Issue 41, 2009, Pages 14650-14651

  Kear, Jamie L ^a   Blackburn, Mandy E ^a   Veloro, Angelo M ^a   Dunn, Ben M ^b   Fanucci, Gail E ^a  

^a University of Florida ^*  (United States)

^b UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ANTIVIRAL THERAPY; CONFORMATIONAL CHANGE; DISTANCE DISTRIBUTIONS; DOUBLE ELECTRON-ELECTRON RESONANCE; ELECTRON PARAMAGNETIC RESONANCE; GAUSSIANS; HIV-1 PROTEASE; HUMAN IMMUNODEFICIENCY VIRUS TYPE-1; POLYPROTEINS; POST-TRANSLATIONAL PROCESSING; SEQUENCE VARIATIONS; SITE-DIRECTED SPIN LABELING; SUBSTRATE BINDING;

BINDING SITES; CONFORMATIONS; ELECTRON RESONANCE; PARAMAGNETIC RESONANCE; PARAMAGNETISM; SUBSTRATES;

ELECTRON SPIN RESONANCE SPECTROSCOPY;

ENZYME VARIANT; PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; DNA POLYMORPHISM; ENZYME CONFORMATION; ENZYME STRUCTURE; HUMAN IMMUNODEFICIENCY VIRUS 1;

CATALYTIC DOMAIN; HIV PROTEASE; HIV PROTEASE INHIBITORS; ISOENZYMES; MODELS, MOLECULAR; POLYMORPHISM, GENETIC;

EID: 70350052784     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja907088a     Document Type: Article

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