Capturing intrinsic nanomechanics of allostery.

Journal Article (Journal Article)

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 Žoldák 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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Duke Authors

Marszalek, Piotr E.

Cited Authors

Marszalek, PE

Published Date

December 2022

Published In

Biophysical Journal

Volume / Issue

121 / 23

Start / End Page

4415 - 4416

PubMed ID

36815705

Pubmed Central ID

PMC9748355

Electronic International Standard Serial Number (EISSN)

1542-0086

International Standard Serial Number (ISSN)

0006-3495

Digital Object Identifier (DOI)

10.1016/j.bpj.2022.10.037

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