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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 2: Focus: Soft Matter and Nanocomposites - New opportunities with advanced neutron sources I
CPP 2.8: Vortrag
Montag, 16. März 2020, 12:00–12:15, ZEU 222
Protein Denaturing Studied by Neutron Scattering: Static and Dynamic Behaviour — •Olga Matsarskaia1, Lena Bühl1,2, Christian Beck1,2, Felix Roosen-Runge3, Marco Grimaldo1, Ralf Schweins1, Fajun Zhang2, Tilo Seydel1, and Frank Schreiber2 — 1Institut Laue-Langevin, Grenoble, France — 2University of Tübingen, Germany — 3Malmö University, Malmö, Sweden
Studying thermal protein denaturing provides valuable information on structural and dynamic aspects related to protein function. Here, we present a combined study of small-angle and quasielastic neutron scattering (SANS and QENS) to shed light on the denaturing of bovine serum albumin (BSA). To obtain insights into the influence of different parameters on protein denaturing, temperature, crowding and charge screening by NaCl are used as control parameters. SANS allows us to obtain global structural and kinetic information on the systems investigated. In addition, QENS data yield mean-squared displacement (MSD) values [1], describing the diffusive behaviour of BSA throughout denaturing. We observe that, while the pathway towards the denatured state is unchanged in the presence of salt, the dynamics of the denatured state itself changes upon the addition of NaCl. Our results offer a framework for a comprehensive, multi-method characterisation of thermal protein denaturing [2].
[1] Hennig et al., Soft Matter (8), 2012, 1628-1633.
[2] Matsarskaia et al., in preparation.