Hsp70 biases the folding pathways of client proteins

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

Volumn 113, Issue 20, 2016, Pages E2794-2801

  Sekhar, Ashok ^a,b   Rosenzweig, Rina ^a,b,c   Bouvignies, Guillaume ^d,e   Kay, Lewis E ^a,b,f  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^d ECOLE NORMALE SUPÉRIEURE   (France)

^e Centre National de la Recherche Scientifique   (France)

^f HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

Excited states; Hsp70; Molecular chaperones; PRE; Protein folding

Indexed keywords

HEAT SHOCK PROTEIN 70; PROTEIN DNAK; TELOMERIC REPEAT BINDING FACTOR 1; UREA; PROTEIN BINDING;

ARTICLE; ENERGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PARAMAGNETIC RELAXATION ENHANCEMENT NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; CHEMISTRY; HUMAN; KINETICS; PHYSIOLOGY; THERMODYNAMICS;

HSP70 HEAT-SHOCK PROTEINS; HUMANS; KINETICS; PROTEIN BINDING; PROTEIN FOLDING; TELOMERIC REPEAT BINDING PROTEIN 1; THERMODYNAMICS;

EID: 84969972739     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1601846113     Document Type: Article

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