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Article

Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding.

Chembiochem : a European journal of chemical biology - 4 Jul 2011

Schweizer Regina S, Aponte Raphael A, Zimmermann Sabine, Weber Annika, Reinstein Jochen

Abstract excerpt

DnaK is a member of the Hsp70 family of molecular chaperones. This molecular machine couples the binding and hydrolysis of ATP to binding and release of substrate proteins. The switches that are involved in allosteric communication within this multidomain protein are mostly unknown. Previous insights were largely obtained by mutants, which displayed either wild-type activity or reduced folding assistance of...

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PMID: 21656889
DOI: 10.1002/cbic.201000786

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding.PMID 21656889Read ↗

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