Chemical and hydrodynamic alignment of an enzyme

Adeleke-Larodo, T.; Agudo-Canalejo, Jaime; Golestanian, Ramin

doi:10.1063/1.5081717

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Chemical and hydrodynamic alignment of an enzyme

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Agudo-Canalejo, Jaime
Department of Living Matter Physics, Max Planck Institute for Dynamics and Self-Organization, Max Planck Society;

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Golestanian, Ramin
Department of Living Matter Physics, Max Planck Institute for Dynamics and Self-Organization, Max Planck Society;

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Citation

Adeleke-Larodo, T., Agudo-Canalejo, J., & Golestanian, R. (2019). Chemical and hydrodynamic alignment of an enzyme. The Journal of Chemical Physics, 150(11): 11502. doi:10.1063/1.5081717.

Cite as: https://hdl.handle.net/21.11116/0000-0003-4053-7

Abstract

Motivated by the implications of the complex and dynamic modular geometry of an enzyme on its motion, we investigate the effect of combining long-range internal and external hydrodynamic interactions due to thermal fluctuations with short-range surface interactions. An asymmetric dumbbell consisting of two unequal subunits, in a nonuniform suspension of a solute with which it interacts via hydrodynamic interactions as well as non-contact surface interactions, is shown to have two alignment mechanisms due to the two types of interactions. In addition to alignment, the chemical gradient results in a drift velocity that is modified by hydrodynamic interactions between the constituents of the enzyme.