Autoprocessing of HIV-1 protease is tightly coupled to protein folding

Nature Structural Biology

Volumn 6, Issue 9, 1999, Pages 868-875

  Louis, John M ^a   Marius Clore, G ^a   Gronenborn, Angela M ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; POL PROTEIN; PROTEINASE; VIRUS PROTEIN;

ARTICLE; DISSOCIATION CONSTANT; ENZYME ACTIVITY; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; VIRUS REPLICATION;

AMINO ACID SEQUENCE; DIMERIZATION; ENZYME ACTIVATION; ENZYME PRECURSORS; ENZYME STABILITY; GENE EXPRESSION REGULATION, VIRAL; HIV PROTEASE; HIV-1; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT FUSION PROTEINS; THERMODYNAMICS;

EID: 17444392445     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/12327     Document Type: Article

References (12)

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