Regensburg 2010 – scientific programme
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 46: Focus: Charge Effects in Soft and Biological Matter II (jointly with BP)
CPP 46.5: Talk
Thursday, March 25, 2010, 15:15–15:30, H37
Charge effects in protein diffusion — •Marcus Hennig1,2, Felix Roosen-Runge2, Fajun Zhang2, Tilo Seydel1, and Frank Schreiber2 — 1Institut Laue-Langevin, Grenoble, France — 2Institut für Angewandte Physik, Universität Tübingen, Germany
Proteins in solution form highly monodisperse colloidal suspensions. Hence, protein solutions are of fundamental interest in a context of soft matter science. A distinguishing feature to simple colloidal systems is the inhomogeneous surface charge distribution of proteins, which is assumed to have a fundamental biological relevance in controlling for instance aggregation phenomena and docking processes. In their native environment proteins are embedded in a crowded solution of various macromolecules and salt ions. These salt ions are crucial for the understanding of the effective interactions of proteins and the dynamics. We study the self-diffusion of the model globular protein Bovine Serum Albumin in aqueous solutions with different salt concentrations by quasi-elastic neutron scattering performed at selected temperatures and in high protein concentrations. Furthermore, by using spin-echo spectroscopy we investigate the collective diffusion behavior. We found that trivalent salts, particularly yttrium chloride, have a pronounced effect on the self and collective diffusion on a nanosecond time scale. Whereas monovalent and divalent salts, such as sodium chloride and calcium chloride, exhibit little or no effect, we observe that the diffusion decreases nearly 50% for a 19mM yttrium chloride concentration.