Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration

Journal of Biological Chemistry

Volumn 271, Issue 10, 1996, Pages 5458-5463

  Szeltner, Zoltán ^a   Polgâr, Lâszlô ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PROTEINASE; SODIUM CHLORIDE; UREA; VIRUS ENZYME;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DENATURATION; ENZYME STABILITY; FLUORESCENCE; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING;

AMINO ACID SEQUENCE; CALORIMETRY; CATALYSIS; CIRCULAR DICHROISM; CLONING, MOLECULAR; ENZYME STABILITY; HIV PROTEASE; HIV-1; HUMANS; HYDROGEN-ION CONCENTRATION; ISOELECTRIC FOCUSING; KINETICS; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; OSMOLAR CONCENTRATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; THERMODYNAMICS; UREA;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0029913459     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.10.5458     Document Type: Article

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