Studying thermal protein denaturation as a nanoscopic structure-dynamics relationship
We will address the process of thermal denaturation in a combined structural-dynamical study using SANS at D11 and QENS at IN16B. In particular, we will use different kind of additives (denaturants, multivalent and monovalent salts) to selectively enhance the propensity of unfolding and cross-linking. The protein BSA is a good choice for this study, since results from complementary techniques provide a solid starting point for this study on the nanoscopic structure-dynamics relationship. We have successfully explored the possibility for this kind of study in a test run at D11, and a previous experiment (exp. 8-04-752) at IN16B. For SANS, we will monitor both cluster and aggregate formation at low q and unfolding at high q (e.g. via Kratky plot). For QENS, we will employ elastic and inelastic fixed window scans to monitor the change of dynamics during thermal denaturation.
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MATSARSKAIA Olga; BECK Christian; FEUSTEL Michal; GRIMALDO Marco; MAIER Ralph; MIKORSKI Marcus; ROOSEN RUNGE Felix; Frank Schreiber; SCHWEINS Ralf; SEYDEL Tilo; SOHMEN Benedikt and ZHANG Fajun. (2016). Studying thermal protein denaturation as a nanoscopic structure-dynamics relationship. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-637
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