Amplitudes and timescales of intrinsically disordered protein dynamics

by Dr. Hagen Hofmann

Department of Chemical and Structural Biology, Weizmann Institute of Science
at Biological and soft-matter physics

Thu, 07 Apr 2022, 12:10
Sacta-Rashi Building for Physics (54), room 207


The dynamics of folded proteins include concerted motions of
thousands of atoms, thus clearly
exceeding the capabilities of
analytical theories. On the other
hand, intrinsically
disordered proteins (IDPs) are well described by analytic polymer models of different flavors. Yet, these models are not applicable if disorder and order mix, e.g., for IDPs that form partially ordered complexes or for disordered linkers that connect folded domains. Using multi-parameter single-molecule FRET, we therefore monitored the dynamics in two partially disordered systems, the E-cadherin/-catenin complex and the enzyme QSOX, at timescales from nanoseconds to milliseconds. We found that many weak interactions cause rugged energy landscapes that slow-down dynamics by orders of magnitude compared to classical IDPs. While the dynamics of the disordered complex are characterized by a single timescale, the dynamics of the enzyme follow power laws due to a mixing of different timescales. I will discuss the potential biological function of the slow dynamics for both molecular systems.

Created on 04-04-2022 by Feingold, Mario (mario)
Updaded on 04-04-2022 by Feingold, Mario (mario)