Viscosity and diffusion: crowding and salt effects in protein solutions

Autor: Michael Sztucki, Marcus Hennig, Fajun Zhang, Fabio Zanini, Frank Schreiber, Felix Roosen-Runge, Ralf Schweins, Marián Antalík, Marco Heinen, Diana Fedunova, Tilo Seydel, Gerhard Nägele

Publikováno v: Soft Matter
Soft Matter, Royal Society of Chemistry, 2012, 8 (5), pp.1404-1419. ⟨10.1039/c1sm06242e⟩
Soft matter 8(5), 1404-1419 (2012). doi:10.1039/c1sm06242e

We report on a joint experimental–theoretical study of collective diffusion in, and static shear viscosity of solutions of bovine serum albumin (BSA) proteins, focusing on the dependence on protein and salt concentration. Data obtained from dynamic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29c5093624057d658e690fc94d8f21a8
https://doi.org/10.1039/c1sm06242e

Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution

Autor: Frank Schreiber, Fajun Zhang, Felix Roosen-Runge, Niina Jalarvo, Marcus Hennig, Tilo Seydel, Michaela Zamponi, Marco Grimaldo, Fabio Zanini

Publikováno v: The journal of physical chemistry letters 6(13), 2577-2582 (2015). doi:10.1021/acs.jpclett.5b01073
The Journal of Physical Chemistry Letters
The Journal of Physical Chemistry Letters, 2015, 6 (13), pp.2577-2582. ⟨10.1021/acs.jpclett.5b01073⟩
'Journal of Physical Chemistry Letters ', vol: 6, pages: 2577-2582 (2015)

The short-time self-diffusion D of the globular model protein bovine serum albumin in aqueous (D2O) solutions has been measured comprehensively as a function of the protein and trivalent salt (YCl3) concentration, noted cp and cs, respectively. We ob

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21e82b58664dd0e3e93f1b6d86d1e08b
https://juser.fz-juelich.de/record/255680

Proline induced disruption of the structure and dynamics of water

Autor: Cheryl Wheeler, Marcus Hennig, Gordon J. Kearley, Richard A. Mole, Jichen Li, Dehong Yu, Thierry Strässle

Publikováno v: Physical chemistry chemical physics : PCCP. 15(47)

We use quasi-elastic neutron scattering spectroscopy to study the diffusive motion of water molecules at ambient temperature as a function of the solute molar fraction of the amino acid, proline. We validate molecular dynamics simulations against exp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58404fe56895823bbae753c7575b8611
https://pubmed.ncbi.nlm.nih.gov/24177249

Protein self-diffusion in crowded solutions

Autor: Felix Roosen-Runge, Frank Schreiber, Robert M. J. Jacobs, Michael Sztucki, Tilo Seydel, Fajun Zhang, Marcus Hennig, Helmut Schober

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2011, 108 (29), pp.11815-11820. ⟨10.1073/pnas.1107287108⟩

Macromolecular crowding in biological media is an essential factor for cellular function. The interplay of intermolecular interactions at multiple time and length scales governs a fine-tuned system of reaction and transport processes, including parti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17833da1274d1cee60671d33e2d734e3
http://ora.ox.ac.uk/objects/uuid:a33f8405-9449-4b12-ac86-630114fbfa20

High-resolution neutron spectroscopy on protein solution samples

Autor: Felix Roosen-Runge, Fajun Zhang, Marcus Hennig, Marco Grimaldo, Frank Schreiber, Michaela Zamponi, Niina Jalarvo, Tilo Seydel, Fabio Zanini

Publikováno v: The European physical journal / Web of Conferences 83, 02005 (2015). doi:10.1051/epjconf/20158302005
EPJ Web of Conferences
EPJ Web of Conferences, EDP Sciences, 2015, 83, pp.02005. ⟨10.1051/epjconf/20158302005⟩
EPJ Web of Conferences, Vol 83, p 02005 (2015)
Les Ulis : EDP Sciences, The @European physical journal / Web of Conferences 83, 02005 pp. (2015). doi:10.1051/epjconf/20158302005
'EPJ Web of Conferences ', vol: 83, pages: 02005-1-02005-6 (2015)

Proteins in solution move subject to a complex superposition of global translational and rotational diffusion as well as internal relaxations covering a wide range of time scales. With the advent of new high-flux neutron spectrometers in combination

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b04789558659ca44e4be4249ffa832de
https://doi.org/10.1051/epjconf/20158302005