The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL
Author:
Publisher
Elsevier BV
Subject
General Biochemistry, Genetics and Molecular Biology
Reference41 articles.
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2. The protein folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer;Azem;Proc. Natl. Acad. Sci. USA,1995
3. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy;Baker;J. Struct. Biol.,1996
4. ATP induces non-identity of two rings in chaperonin GroEL;Bochkareva;J. Biol. Chem.,1994
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