Unravelling protein dynamics by combining single-molecule fluorescence, MD simulations and quasi-elastic neutron scattering

General ILL Webinar 

Organised by College 8

Friday 18th February 2022 at 11h00

Zoom link here | Passcode : 765953

Dr. Benedikt Sohmen | Institute of Physical Chemistry, Freiburg University, Germany

Understanding protein function requires to complement structural information with dynamics information. Here, we unravel nanosecond dynamics for the multi-domain protein and chaperone Hsp90 using single-molecule fluorescence, MD simulations and quasi-elastic neutron scattering [1, 2]. As a molecular chaperone and ATPase with hundreds of client proteins, Hsp90 developed into a promising drug target [3]. Our integrative approach allows us to disentangle local from global dynamics of Hsp90,revealing internal dynamics on the 100 nanosecond time scale. We find that these internal dynamics are molecule-spanning and, interestingly, can be influenced by Sba1, a co-chaperone of Hsp90. Altogether, our results suggest the nanosecond time scale to be a potentially underestimated level of protein regulation.

[1] Sohmen et al., https://arxiv.org/abs/2110.10483

[2] Wolf et al., Chem.Sci. 12 (2021) 3350 - 3359

[3] Schopf et al., Nat.Rev. 18 (2017) 345–360

Olga Matsarskaia (College 8 secretary)