Regensburg 2016 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 23: Posters - Protein Structure and Dynamics
BP 23.2: Poster
Montag, 7. März 2016, 17:30–19:30, Poster C
Protein folding investigated by SANS/SAXS small angle scattering and neutron spin-echo — •Felix Ameseder1, Aurel Radulescu2, Olaf Holderer2, Andreas Stadler1, and Dieter Richter1 — 1Forschungszentrum Jülich GmbH, Neutron Scattering, JCNS/ICS-1 — 2Forschungszentrum Jülich GmbH, Neutron Scattering, JCNS-FRMII
The process of protein folding is highly dependent on the amino acid composition as well as on the solution condition, especially on the presence of denaturant. Our approach is to describe the folding by coefficient dimension of polymer scaling laws, and measure the folding as a function of denaturant type and denaturant concentration which has proved to be promising in singlemolecule FRET experiments. Here, we use SANS/SAXS to determine the structure of bovine serum albumin m=66kD in H20/D2O buffer solution and at various concentrations of guanidine hydrochloride and β-mercaptoethanol as additional solvent. The global dynamics of native and unfolded BSA is investigated with dynamic light scattering spectroscopy. The advantage of neutron spin-echo spectroscopy is used to cover a time range up to 140ns with spacial resolution from q=0.05A−1 to q=0.17A−1. SANS and SAXS results of native BSA show agreement with coherent scattering intensities calculated from crystal structure model of a respective monomer. All scattering data of unfolded structures reveal distinct evidence of the lost of internal order. NSE measurements of disordered structures reveal a contribution of internal dynamics to global diffusion.