Unfolding and Disassembly of the Chaperonin GroEL Occurs via a Tetradecameric Intermediate with a Folded Equatorial Domain
Author:
Affiliation:
1. Department of Chemistry and Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska, Lincoln, Nebraska 68588-0304
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi992619n
Reference46 articles.
1. STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
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2. Folding and unfolding pathway of chaperonin GroEL monomer and elucidation of thermodynamic parameters;International Journal of Biological Macromolecules;2017-03
3. Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins;Biophysical Chemistry;2016-01
4. Key factors in chaperonin-assisted protein folding;Particuology;2012-02
5. Med8, Med18, and Med20 subunits of the Mediator head domain are interdependent upon each other for folding and complex formation;Proceedings of the National Academy of Sciences;2009-11-23
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