The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG

Protein Science

Volumn 12, Issue 11, 2003, Pages 2588-2596

  Stevens, Shawn Y ^a   Cai, Sheng ^a   Pellecchia, Maurizio ^a,c   Zuiderweg, Erik R P ^a,b  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c BURNHAM INSTITUTE   (United States)

Author keywords

Allosteric; DnaK; Dynamics; Hsp70; NMR; Solution structure

Indexed keywords

ASPARAGINYLARGINYLLEUCYLLEUCYLLEUCYLTHREONYLGLYCINE; CHAPERONE; HEAT SHOCK PROTEIN 70; UNCLASSIFIED DRUG;

ALLOSTERISM; ALPHA HELIX; ARTICLE; BINDING KINETICS; BINDING SITE; COMPLEX FORMATION; CRYSTAL STRUCTURE; MOLECULAR DYNAMICS; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; STRUCTURE ANALYSIS;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SOLUTIONS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0142148040     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03269103     Document Type: Article

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