BPCPPDYSOE21 – wissenschaftliches Programm
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DY: Fachverband Dynamik und Statistische Physik
DY 45: Brownian Motion and Anomalous Transport - organized by Ralf Metzler (Potsdam)
DY 45.2: Vortrag
Mittwoch, 24. März 2021, 14:30–14:50, DYc
Cooperatively enhanced reactivity and stabilitaxis of dissociating oligomeric proteins — •Jaime Agudo-Canalejo1, Pierre Illien2, and Ramin Golestanian1 — 1Department of Living Matter Physics, Max Planck Institute for Dynamics and Self-Organization, Göttingen, Germany — 2Sorbonne Universite, CNRS, Laboratoire PHENIX, UMR CNRS 8234, Paris, France
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 on them a functional advantage with respect to non-dissociating proteins [1]. 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 localized targets. In non-uniform environments with position-dependent association-dissociation, caused by, for example, 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."
[1] Agudo-Canalejo, J., Illien, P., & Golestanian, R. (2020). Proceedings of the National Academy of Sciences, 117(22), 11894-11900.