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Biochemical hydrodynamics of protein solutions with high pressure relaxation kinetics

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If you have a question about this talk, please contact Dr Ed Brambley.

This work aims to formulate a rational approach to problems of biochemical hydrodynamics of protein-solvent systems. The common feature of such problems is the existence of the myriad of simultaneous biochemical reactions with a broadband distribution of reaction rates. Normally, the kinetic events can be initiated by the disturbance of the system from the state of thermodynamic equilibrium either via the perturbation of the pressure, the temperature or the chemical content of the solution. This work considers the case of pressure induced relaxation kinetics.

Typically, biochemical studies do not consider the effects of interaction between hydrodynamic motions and kinetics. Being primarily concerned with calculations of the reaction rates and other important characteristics of the involved biochemical processes, they represent the fluid state by means of effective steadystate values. However, when the relaxation times of the involved microscopic kinetics occupy a broadband interval, hydrodynamic and kinetic time scales may become comparable. In this situation the hydrodynamic state cannot be treated as passive to the kinetic changes. Neither can the effects of kinetics on the hydrodynamics be schematically represented by a small number of relaxation equations, since this would contradict the broadband nature of the involved kinetics. Consequently, one enters into a new area of hydrodynamics in which modelling of the interaction between the broadband protein kinetics and nonequilibrium fluid motion is required. This work illustrates the distinctive features of this new class of problems by considering the practically important example of pressure initiated fast relaxation kinetics in protein solutions.

Owing to the broadband distribution of the reaction rates, the approach to modelling based on a large number of ordinary differential equations of reaction kinetics is impractical as it results in a stiff system of governing equations. An alternative method is to use continuous distributions of relaxation times, in order to account for the kinetic effects. This approach results in a compact set of equations similar to the conventional Navier-Stokes-Fourier system, but with additional terms responsible for the production of entropy owing to the biochemical changes of the medium’s structure.

This talk analyzes one such methodology from the point of view of novel hydrodynamic effects caused by pressure induced fast protein kinetics which would not be observed if conventional equations of fluid mechanics were used.

This talk is part of the Fluid Mechanics (DAMTP) series.

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