Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system

Protein Science

Volumn 21, Issue 10, 2012, Pages 1489-1502

  Sekhar, Ashok ^a,b   Lam, Hon Nam ^a   Cavagnero, Silvia ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

Chaperone substrate interactions; DnaJ; DnaK; GrpE; Hsp70; Kinetic partitioning; Protein folding

Indexed keywords

HEAT SHOCK PROTEIN 70; PEPTIDES AND PROTEINS; PROTEIN DNAJ; PROTEIN DNAK; PROTEIN GRPE; RIBONUCLEASE; UNCLASSIFIED DRUG;

ARTICLE; CHAMP70; ENZYME KINETICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; THERMODYNAMICS;

ADENOSINE TRIPHOSPHATE; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; KINETICS; MODELS, MOLECULAR; PROTEIN FOLDING; REPRODUCIBILITY OF RESULTS; SOFTWARE; THERMODYNAMICS;

EID: 84866621300     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2139     Document Type: Article

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