Journal
BIOPHYSICAL JOURNAL
Volume 121, Issue 23, Pages 4415-4416Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2022.10.037
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Funding
- NSF
- [MCB 1817556]
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In this article, Singh, Rief, and Zoldak provide an exquisitely detailed study of the nanomechanical aspects of the allosteric mechanism in the Hsp70 chaperone DnaK.
The Hsp70 chaperone exploits allosteric communication between its substrate binding domain and its nucleotide binding domain to regulate the loading and release of misfolded polypeptides in an ATP-hydrolysis-dependent manner. In this issue of Biophysical Journal, Singh, Rief, and Zoldak report an exquisitely detailed study of the nanomechanical aspects of the allosteric mechanism in DnaK, an Escherichia coli heat shock protein 70 chaperone.
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