Capturing intrinsic nanomechanics of allostery

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.

Automated summary

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.