Diffusion in protein solutions: the effect of crowding, temperature and charges
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.
Publications
- (2014) Diffusion and Dynamics of γ-Globulin in Crowded Aqueous Solutions. The Journal of Physical Chemistry B 118:7203-7209
Grimaldo M, Roosen-Runge F, Zhang F, Seydel T, Schreiber F
(See online at https://doi.org/10.1021/jp504135z) - (2015) Hierarchical molecular dynamics of bovine serum albumin in concentrated aqueous solution below and above thermal denaturation. Phys. Chem. Chem. Phys. 17:4645-4655
Grimaldo M, Roosen-Runge F, Hennig M, Zanini F, Zhang F, Jalarvo N, Zamponi M, Schreiber F, Seydel T
(See online at https://doi.org/10.1039/c4cp04944f) - (2015) High-resolution neutron spectroscopy on protein solution samples. EPJ Web of Conferences 83
Grimaldo M, Roosen-Runge F, Jalarvo N, Zamponi M, Zanini F, Hennig M, Zhang F, Schreiber F, Seydel T
(See online at https://dx.doi.org/10.1051/epjconf/20158302005) - (2015) Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution. The Journal of Physical Chemistry Letters 6:2577-2582
Grimaldo M, Roosen-Runge F, Hennig M, Zanini F, Zhang F, Zamponi M, Jalarvo N, Schreiber F, Seydel T
(See online at https://doi.org/10.1021/acs.jpclett.5b01073) - (2016) Global and Internal Diffusive Dynamics of Proteins in Solution studied by neutron spectroscopy, PhD Dissertation. Universität Tübingen, Tübingen
Grimaldo M.
(See online at https://dx.doi.org/10.15496/publikation-12789) - (2017) Crowding-Controlled Cluster Size in Concentrated Aqueous Protein Solutions: Structure, Self- and Collective Diffusion. The Journal of Physical Chemistry Letters 8:2590-2596
Braun MK, Grimaldo M, Roosen-Runge F, Hoffmann I, Czakkel O, Sztucki M, Zhang F, Schreiber F, Seydel T
(See online at https://doi.org/10.1021/acs.jpclett.7b00658) - (2017) Strong Isotope Effects on Effective Interactions and Phase Behavior in Protein Solutions in the Presence of Multivalent Ions. The Journal of Physical Chemistry B 121:1731-1739
Braun MK, Wolf M, Matsarskaia O, Da Vela S, Roosen-Runge F, Sztucki M, Roth R, Zhang F, Schreiber F
(See online at https://doi.org/10.1021/acs.jpcb.6b12814) - (2018) Effective interaction, Global dynamics and cluster formation in protein solutions, PhD Dissertation. Universität Tübingen, Tübingen
Braun, M.K.
