Electrostatic analysis of the hepatitis C virus NS3 helicase reveals both active and allosteric site locations

Nucleic Acids Research

Volumn 32, Issue 18, 2004, Pages 5519-5528

  Frick, David N ^a   Rypma, Ryan S ^a   Lam, Angela M I ^a   Frenz, Christopher M ^a  

^a NEW YORK MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; NUCLEIC ACID; RNA HELICASE; NS3 PROTEIN, HEPATITIS C VIRUS; VIRUS PROTEIN;

ARTICLE; BINDING SITE; CONTROLLED STUDY; ELECTRICITY; ENZYME ANALYSIS; ENZYME STRUCTURE; HEPATITIS C VIRUS; IONIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; CHEMISTRY; GENETICS; METABOLISM; PH; PROTEIN CONFORMATION;

HEPATITIS C VIRUS;

ALLOSTERIC SITE; BINDING SITES; ELECTROSTATICS; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RNA HELICASES; VIRAL NONSTRUCTURAL PROTEINS;

EID: 6044262451     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh891     Document Type: Article

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