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DY: Fachverband Dynamik und Statistische Physik
DY 26: Brownian Motion, Transport and Anomalous Diffusion
DY 26.4: Vortrag
Dienstag, 17. März 2020, 10:45–11:00, HÜL 186
Cooperatively enhanced reactivity and stabilitaxis of dissociating oligomeric proteins — •Jaime Agudo-Canalejo1, Pierre Illien2, and Ramin Golestanian1,3 — 1Max Planck Institute for Dynamics and Self-Organization (MPIDS), D-37077 Göttingen, Germany — 2Sorbonne Université, CNRS, Laboratoire PHENIX, UMR CNRS 8234, 75005 Paris, France — 3Rudolf Peierls Centre for Theoretical Physics, University of Oxford, Oxford OX1 3PU, United Kingdom
Many functional units in biology, such as enzymes or molecular motors, are composed of several subunits that can reversibly assemble and disassemble. This includes oligomeric proteins composed of several smaller monomers, as well as protein complexes assembled from a few proteins. By studying the generic spatial transport properties of such proteins, we investigate here whether their ability to reversibly associate and dissociate may confer them a functional advantage with respect to nondissociating proteins. In uniform environments with position-independent association-dissociation, we find that enhanced diffusion in the monomeric state coupled to reassociation into the functional oligomeric form leads to enhanced reactivity with distant targets. In non-uniform environments with position-dependent association-dissociation, caused e.g. by spatial gradients of an inhibiting chemical, we find that dissociating proteins generically tend to accumulate in regions where they are most stable, a process that we term 'stabilitaxis'.