Chemical and hydrodynamic alignment of an enzyme

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...

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Huvudupphovsmän: Adeleke-Larodo, T, Agudo-Canalejo, J, Golestanian, R
Materialtyp: Journal article
Språk:English
Publicerad: AIP Publishing 2019
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author Adeleke-Larodo, T
Agudo-Canalejo, J
Golestanian, R
author_facet Adeleke-Larodo, T
Agudo-Canalejo, J
Golestanian, R
author_sort Adeleke-Larodo, T
collection OXFORD
description 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.
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spelling oxford-uuid:bc8da60a-d7ed-4fc7-8bf6-9d3fe04a3cb32022-03-27T05:25:11ZChemical and hydrodynamic alignment of an enzymeJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:bc8da60a-d7ed-4fc7-8bf6-9d3fe04a3cb3EnglishSymplectic Elements at OxfordAIP Publishing2019Adeleke-Larodo, TAgudo-Canalejo, JGolestanian, RMotivated 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.
spellingShingle Adeleke-Larodo, T
Agudo-Canalejo, J
Golestanian, R
Chemical and hydrodynamic alignment of an enzyme
title Chemical and hydrodynamic alignment of an enzyme
title_full Chemical and hydrodynamic alignment of an enzyme
title_fullStr Chemical and hydrodynamic alignment of an enzyme
title_full_unstemmed Chemical and hydrodynamic alignment of an enzyme
title_short Chemical and hydrodynamic alignment of an enzyme
title_sort chemical and hydrodynamic alignment of an enzyme
work_keys_str_mv AT adelekelarodot chemicalandhydrodynamicalignmentofanenzyme
AT agudocanalejoj chemicalandhydrodynamicalignmentofanenzyme
AT golestanianr chemicalandhydrodynamicalignmentofanenzyme