Cooperative Assembly of Hsp70 Subdomain Clusters

Maya A. Wright, Francesco A. Aprile, Mathias M. J. Bellaiche, Thomas C. T. Michaels, Thomas Müller, Paolo Arosio, Michele Vendruscolo, Christopher M. Dobson, and Tuomas P. J. Knowles

Biochemistry, 2018 May 15

In this paper, Wright et al use Microfluidic Diffusional Sizing (MDS) to study the oligomerization of SBD641, the substrate binding subdomain of human Hsp70. By revealing the thermodynamic parameters governing the oligomerization, they show structural constraints on the oligomer size are likely determined by specific molecular interaction modes at the interface.

Wright et al Hsp70 abstract figure

While it is known that molecular chaperones play a crucial role in assisting protein folding, the authors note that existing analysis techniques are better suited to testing monodisperse solutions of isolated components - so MDS has offered a new avenue for these types of tests.

Measurements of the unlabelled sample were conducted using a Fluidity One instrument in order to verify that the fluorescent label used in the study did not affect the measured hydrodynamic radius.