Local unfolding of the HSP27 monomer regulates chaperone activity
T. R. Alderson, J. Roche, H. Y. Gastall, I. Pritisanac, J. Ying, A. Bax, J. L. P. Benesch, A. J. Baldwin
This study shows that redox-induced monomerization of HSP27 enhances its chaperone activity but also increases aggregation risk, with mutations in an unstructured region linked to neuropathies.
bioRxiv · Jun 14, 2018Biophysics