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Chemical and hydrodynamic alignment of an enzyme

MPG-Autoren
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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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Zitation

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.


Zitierlink: https://hdl.handle.net/21.11116/0000-0003-4053-7
Zusammenfassung
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.