Chemical and hydrodynamic alignment of an enzyme
arXiv:1811.09631 · doi:10.1063/1.5081717
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.
arXiv comment7+4 pages, 3 figures
References in corpus (9)
- Clusters, asters and collective oscillations in chemotactic colloids
- 'Fuelled' motion: phoretic motility and collective behaviour of active colloids
- Enhanced Diffusion of Enzymes that Catalyze Exothermic Reactions
- Hydrodynamic Collective Effects of Active Protein Machines in Solution and Lipid Bilayers
- Phoresis and Enhanced Diffusion Compete in Enzyme Chemotaxis
- Exothermicity is not a necessary condition for enhanced diffusion of enzymes
- Enhanced diffusion and chemotaxis at the nanoscale
- Synthetic Mechanochemical Molecular Swimmer
- Diffusion of an Enzyme: the Role of Fluctuation-Induced Hydrodynamic Coupling
Cited by in corpus (7)
- Nonequilibrium polarity-induced mechanism for chemotaxis: emergent Galilean symmetry and exact scaling exponents
- Non-equilibrium phase separation in mixtures of catalytically active particles: size dispersity and screening effects
- Exact axisymmetric interaction of phoretically active Janus particles
- Hydrodynamics of an odd active surfer in a chiral fluid
- Nonequilibrium Transport Induced by Biological Nanomachines
- Diffusion and steady state distributions of flexible chemotactic enzymes
- Comment on "Relative Diffusivities of Bound and Unbound Protein Can Control Chemotactic Directionality''