Structural properties of the histidine-containing loop in HIV-1 RNase H

Biophysical Chemistry

Volumn 96, Issue 2-3, 2002, Pages 285-291

  Kern, Gunther ^a,b   Pelton, Jeff ^a   Marqusee, Susan ^a   Kern, Dorothee ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b ASTRAZENECA   (United Kingdom)

Author keywords

His; HIV 1 RNase H; NMR; Protein folding; Reverse transcriptase

Indexed keywords

HISTIDINE; RIBONUCLEASE; VIRUS ENZYME; RIBONUCLEASE H; UREA;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATION; CONTROLLED STUDY; GENE DELETION; HUMAN IMMUNODEFICIENCY VIRUS 1; MUTANT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS; CHEMISTRY; DRUG EFFECT; ENZYMOLOGY; HUMAN; PH; PROTEIN CONFORMATION; PROTEIN DENATURATION; STRUCTURE ACTIVITY RELATION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

HISTIDINE; HIV-1; HUMANS; HYDROGEN-ION CONCENTRATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; RIBONUCLEASE H, CALF THYMUS; STRUCTURE-ACTIVITY RELATIONSHIP; UREA;

EID: 0037007473     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00019-4     Document Type: Article

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