Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK)

Cell Stress and Chaperones

Volumn 17, Issue 3, 2012, Pages 313-327

  Thompson, Andrea D ^a   Bernard, Steffen M ^a   Skiniotis, Georgios ^a,b   Gestwicki, Jason E ^a,b  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

Allostery; Chaperone; Electron microscopy; Oligomers; Protein complexes

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; DIMER; HEAT SHOCK PROTEIN 70; MONOMER; OLIGOMER; PROTEIN DNAJ; PROTEIN DNAK;

ARTICLE; CONTROLLED STUDY; CROSS LINKING; ELECTRON MICROSCOPY; ESCHERICHIA COLI; GEL ELECTROPHORESIS; HEAT SHOCK; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE STRESS;

ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HSP70 HEAT-SHOCK PROTEINS; KINETICS; NUCLEOTIDES; PROTEIN BINDING; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS;

ESCHERICHIA COLI;

EID: 84863590889     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-011-0307-1     Document Type: Article

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