Symmetric GroEL: GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine

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

Volumn 110, Issue 46, 2013, Pages

  Yang, Dong ^a,b   Ye, Xiang ^a,b   Lorimer, George H ^a,b  

^a UNIVERSITY OF MARYLAND   (United States)

^b University of Maryland   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALPHA LACTALBUMIN; CHAPERONIN; CHAPERONIN 60; EARLY PREGNANCY FACTOR; NUCLEOTIDE; PROTEIN; SUBSTRATE PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; FLUORESCENCE RESONANCE ENERGY TRANSFER; NANOCATALYSIS; NANOENCAPSULATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; STEADY STATE; STOCHASTIC MODEL;

ADENOSINE TRIPHOSPHATE; CHAPERONIN 10; CHAPERONIN 60; FLUORESCENCE RESONANCE ENERGY TRANSFER; GUANOSINE; HYDROLYSIS; KINETICS; MODELS, BIOLOGICAL; MULTIPROTEIN COMPLEXES; PHOSPHATE-BINDING PROTEINS; PROTEIN FOLDING; THIONUCLEOSIDES;

EID: 84887433399     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1318862110     Document Type: Article

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