Denaturation process in protein solutions studied by inelastic fixed window scans
Denaturation in protein solutions combines (partial) unfolding and subsequent aggregation of proteins and depends strongly on the solution conditions. We aim for a systematic investigation of hierarchical dynamics during the thermal denaturation process of bovine serum albumin (BSA) using inelastic fixed window scans at IN16B. The experiment will elucidate the process of unfolding and cross-linking during thermal denaturation. Using different protein and salt concentrations, the interplay between steric and Coulomb repulsion and emerging attractions during denaturation will be explored. Importantly, neutron backscattering at IN16B extends the picture of hierarchical dynamics during denaturation down to the otherwise unaccessible nanoscale. Furthermore, the experiment will present a first showcase for protein condensation under physiological conditions, which opens the field towards a more detailed characterization of nanoscopic dynamical changes during self-assembly processes.
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ROOSEN RUNGE Felix; FEUSTEL Michal; GRIMALDO Marco; Frank Schreiber; SEYDEL Tilo and ZHANG Fajun. (2015). Denaturation process in protein solutions studied by inelastic fixed window scans. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-752
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