Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR

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

Volumn 112, Issue 29, 2015, Pages 8817-8823

  Libich, David S ^a   Tugarinov, Vitali ^a   Clore, G Marius ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

Chaperonins; Dark state exchange saturation transfer; Invisible states; Lifetime line broadening; Relaxation dispersion

Indexed keywords

CARBON 13; CHAPERONIN 60; DEUTERIUM; ISOTOPE; NITROGEN 15; CARBON; NITROGEN; PROTEIN BINDING;

ARTICLE; ASSOCIATION RATE CONSTANT; BINDING SITE; CATALYSIS; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN UNFOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CHICKEN; KINETICS; METABOLISM; PROTEIN CONFORMATION; SRC HOMOLOGY DOMAIN;

ANIMALS; CARBON ISOTOPES; CHAPERONIN 60; CHICKENS; KINETICS; MODELS, MOLECULAR; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; SRC HOMOLOGY DOMAINS;

EID: 84937468654     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1510083112     Document Type: Article

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