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Diffusion in protein solutions: the effect of crowding, temperature and charges

Subject Area Statistical Physics, Nonlinear Dynamics, Complex Systems, Soft and Fluid Matter, Biological Physics
Term from 2013 to 2017
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 240526267
 
Final Report Year 2018

Final Report Abstract

The research for this project has employed high-resolution neutron spectroscopy as a key method to access both the self- and collective diffusion of model proteins in aqueous solutions. Neutron spectroscopy has been complemented by x-ray and neutron small-angle scattering, dynamic light scattering, and other techniques. The research has resulted in establishing experimental and analytical frameworks to systematically understand protein cluster formation as a function of different sample parameters, such as the crowding-induced cluster formation for the beta-lactoglobulin protein model system, which can be probed by a combination of static (SAXS) and neutron spectroscopic techniques. The combination of these methods allows to infer on clusters with a hydrodynamic size that depends on the protein concentration in solution. In a different system, namely bovine serum albumin in the presence of YCl3, protein clusters are formed depending on the protein cp and salt cs concentration. This cluster formation results in a master curve for the observable cluster short-time self-diffusion coefficient D(cs,cp)=D(cs=0,cp)g(cs/cp) with a scalar function g that only depends on the ratio cs/cp of the salt and protein concentration and can be understood quantitatively in terms of predictions from the theory of so-called patchy colloids.

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