Characterization of two hydrophobic methyl clusters in HIV-1 protease by NMR spin relaxation in solution

Journal of Molecular Biology

Volumn 305, Issue 3, 2001, Pages 515-521

  Ishima, Rieko ^a   Louis, John M ^b   Torchia, Dennis A ^a  

^a NATIONAL INSTITUTE OF DENTAL AND CRANIOFACIAL RESEARCH   (United States)

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

Author keywords

Conformational change; Internal motion; Protein; Retroviral protease

Indexed keywords

METHYL GROUP; PROTEINASE; VIRUS ENZYME;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DRUG BINDING; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN MOTIF; RETROVIRUS;

EID: 0035910284     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4321     Document Type: Article

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