Dresden 2017 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 24: Posters - Protein Structure and Dynamics
BP 24.16: Poster
Dienstag, 21. März 2017, 14:00–16:00, P1A
Effect of disulfide bridges on denatured protein dynamics investigated by neutron spin-echo spectroscopy — •Felix Ameseder1, Aurel Radulescu2, Peter Falus3, Andreas Stadler1, and Dieter Richter1 — 1Forschungszentrum Jülich GmbH, JCNS-1/ICS-1, Germany — 2Forschungszentrum Jülich GmbH, JCNS Outstation at MLZ, Germany — 3Institut Laue-Langevin, France
The dynamics of proteins in solution is highly dependent on the presence of covalent bonds acting as internal crosslinks between different domains.
Here, we investigate the denatured Bovine Serum Albumin (BSA) protein in solution at 6 molar guanidine hydrochloride first with active disulfide bridges, and secondly with reduced disulfide bridges using β-mercaptoethanol as additional chemical denaturant.
The results are interpreted with common polymer models that include hydrodynamic interactions like the Zimm model.
The protein structure was investigate beforehand with small angle neutron scattering SANS and small angle x-ray scattering SAXS. A distinct power law scaling behavior could be retrieved for both cases.
The dynamics of the protein was investigated with dynamic light scattering, and neutron spin-echo spectroscopy NSE. The NSE results reveal distinct differences of the internal dynamics between the both cases that will be discussed in detail in the talk.