The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 28, 2004, Pages 10272-10277

  Zhang, Yongbo ^a   Zuiderweg, Erik R P ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN;

ALLOSTERISM; ANTIGEN PRESENTATION; ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MECHANICS; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION;

ADENOSINE TRIPHOSPHATASES; ALLOSTERIC SITE; ANIMALS; BINDING SITES; CATTLE; CRYSTALLOGRAPHY; HSC70 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEOTIDES; PROTEIN STRUCTURE, TERTIARY;

MAMMALIA;

EID: 3142677815     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0401313101     Document Type: Article

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