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Projekt Druckansicht

Diffusion in Proteinlösungen: Der Einfluß von "Crowding", Temperatur und Ladungen

Fachliche Zuordnung Statistische Physik, Nichtlineare Dynamik, Komplexe Systeme, Weiche und fluide Materie, Biologische Physik
Förderung Förderung von 2013 bis 2017
Projektkennung Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 240526267
 
Erstellungsjahr 2018

Zusammenfassung der Projektergebnisse

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.

Projektbezogene Publikationen (Auswahl)

  • (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
    (Siehe online unter 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
    (Siehe online unter 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
    (Siehe online unter 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
    (Siehe online unter 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.
    (Siehe online unter 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
    (Siehe online unter 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
    (Siehe online unter 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.
 
 

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