Project Details
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Static and dynamic properties of antibody proteins in solution - the effects of crowding and charge-tuning

Subject Area Statistical Physics, Nonlinear Dynamics, Complex Systems, Soft and Fluid Matter, Biological Physics
Experimental Condensed Matter Physics
Term from 2016 to 2021
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 316738961
 
Final Report Year 2021

Final Report Abstract

As a central result, the project has shown that an important contribution to the physical understanding of macromolecular crowding in living systems can be achieved by systematically varying the parameters volume fraction and polydispersity of the crowding, further the temperature, the type of tracer protein, and the salt-induced charge concentration, by employing xray and neutron scattering experiments, and by comparing the results to simulations of polydisperse hard-sphere suspensions. An important aspect of the project consisted in the nanosecond observation time scale, on which hydrodynamic aspects prevail and can be uniquely probed. Understanding these hydrodynamic interactions is a requirement for the description on all longer diffusive time scales.

Publications

  • Effective interactions and colloidal stability of bovine γ-globulin in solution. J. Phys. Chem. B 121 (2017) 5759
    S. Da Vela, F. Roosen-Runge, M. W. A. Skoda, R. M. J. Jacobs, T. Seydel, H. Frielinghaus, M. Sztucki, R. Schweins, F. Zhang, and F. Schreiber
    (See online at https://doi.org/10.1021/acs.jpcb.7b03510)
  • Nanosecond tracer diffusion as a probe of the solution structure and molecular mobility of protein assemblies: The case of ovalbumin. J. Phys. Chem. B 122 (2018) 8343
    C. Beck, M. Grimaldo, F. Roosen-Runge, M. Braun, F. Zhang, F. Schreiber, and T. Seydel
    (See online at https://doi.org/10.1021/acs.jpcb.8b04349)
  • Two time scales for self and collective diffusion near the critical point in a simple patchy model for proteins with floating bonds. Soft Matter 14 (2018) 8006
    J. Bleibel, M. Habiger, M. Lütje, F. Hirschmann, F. Roosen-Runge, T. Seydel, F. Zhang, F. Schreiber, and M. Oettel
    (See online at https://doi.org/10.1039/C8SM00599K)
  • Dynamics of proteins in solution. Quart. Rev. Biophys. 52 (2019) e7, 1
    M. Grimaldo, F. Roosen-Runge, F. Zhang, F. Schreiber, and T. Seydel
    (See online at https://doi.org/10.1017/S0033583519000027)
  • Following protein dynamics in real-time during crystallization. Cryst. Growth Des. 19 (2019) 7036
    C. Beck, M. Grimaldo, F. Roosen-Runge, R. Maier, O. Matsarskaia, M. Braun, B. Sohmen, O. Czakkel, R. Schweins, F. Zhang, T. Seydel, and F. Schreiber
    (See online at https://doi.org/10.1021/acs.cgd.9b00858)
  • Protein short-time diffusion in a naturally crowded environment. J. Phys. Chem. Lett. 10 (2019) 1709
    M. Grimaldo, H. Lopez, C. Beck, F. Roosen-Runge, M. Moulin, J. Devos, V. Laux, M. Härtlein, S. Da Vela, R. Schweins, A. Mariani, F. Zhang, J.L. Barrat, M. Oettel, V.T. Forsyth, T. Seydel, and F. Schreiber
    (See online at https://doi.org/10.1021/acs.jpclett.9b00345)
  • Microscopic Dynamics of Liquid-Liquid Phase Separation and Domain Coarsening in a Protein Solution Revealed by X-Ray Photon Correlated Spectroscopy. Phys.Rev.Lett. 126 (2021) 138004
    A. Girelli, H. Rahmann, N. Begam, A. Ragulskaya, M. Reiser, S. Chandran, F. Westermeier, M. Sprung, F. Zhang, C. Gutt, and F. Schreiber
    (See online at https://doi.org/10.1103/physrevlett.126.138004)
 
 

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