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 ┼Żoldák report an exquisitely detailed study of the nanomechanical aspects of the allosteric mechanism in DnaK, an Escherichia coli heat shock protein 70 chaperone.

Full Text

Duke Authors

Cited Authors

  • Marszalek, PE

Published Date

  • December 2022

Published In

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


  • eng