Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations

Biophysical Journal

Volumn 93, Issue 7, 2007, Pages 2289-2299

  Zheng, Wenjun ^a,c   Brooks, Bernard R ^a   Thirumalai, D ^b  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^b Bldg 142   (United States)

^c UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; LIGAND;

ALLOSTERISM; ARTICLE; CONFORMATIONAL TRANSITION; LIGAND BINDING; PROTEIN DOMAIN; PROTEIN FOLDING;

ESCHERICHIA COLI;

EID: 34848852941     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.105270     Document Type: Article

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