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Capturing intrinsic nanomechanics of allostery.

Publication ,  Journal Article
Marszalek, PE
Published in: Biophysical journal
December 2022

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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Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

December 2022

Volume

121

Issue

23

Start / End Page

4415 / 4416

Related Subject Headings

  • HSP70 Heat-Shock Proteins
  • Escherichia coli Proteins
  • Escherichia coli
  • Biophysics
  • Allosteric Regulation
  • Adenosine Triphosphate
  • 51 Physical sciences
  • 34 Chemical sciences
  • 31 Biological sciences
  • 06 Biological Sciences
 

Citation

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MLA
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Marszalek, P. E. (2022). Capturing intrinsic nanomechanics of allostery. Biophysical Journal, 121(23), 4415–4416. https://doi.org/10.1016/j.bpj.2022.10.037
Marszalek, Piotr E. “Capturing intrinsic nanomechanics of allostery.Biophysical Journal 121, no. 23 (December 2022): 4415–16. https://doi.org/10.1016/j.bpj.2022.10.037.
Marszalek PE. Capturing intrinsic nanomechanics of allostery. Biophysical journal. 2022 Dec;121(23):4415–6.
Marszalek, Piotr E. “Capturing intrinsic nanomechanics of allostery.Biophysical Journal, vol. 121, no. 23, Dec. 2022, pp. 4415–16. Epmc, doi:10.1016/j.bpj.2022.10.037.
Marszalek PE. Capturing intrinsic nanomechanics of allostery. Biophysical journal. 2022 Dec;121(23):4415–4416.
Journal cover image

Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

December 2022

Volume

121

Issue

23

Start / End Page

4415 / 4416

Related Subject Headings

  • HSP70 Heat-Shock Proteins
  • Escherichia coli Proteins
  • Escherichia coli
  • Biophysics
  • Allosteric Regulation
  • Adenosine Triphosphate
  • 51 Physical sciences
  • 34 Chemical sciences
  • 31 Biological sciences
  • 06 Biological Sciences