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BP: Fachverband Biologische Physik
BP 33: Protein Structure and Dynamics
BP 33.2: Vortrag
Donnerstag, 19. März 2020, 09:45–10:00, ZEU 250
Conformational Changes of IDP under Influence of Guanidinium Chloride: Integrative Approach using X-ray/Neutron Scattering and Single Molecule Spectrosopy — •Luman Haris1,2, Livia Balacescu1,2,3, Iwo König4, Martin Dulle1, Aurel Radulescu3, Ingo Hoffmann5, Tobias Erich Schrader3, Ben Schuler4, and Andreas Maximilian Stadler1,2 — 1FZ Jülich, JCNS-1 & ICS-1, Jülich — 2IPC, RWTH Aachen, Aachen — 3FZ Jülich, Outstation MLZ, Garching — 4Biochemisches Institut, Universität Zürich, Zürich — 5Institut Laue-Langevin, Grenoble
IDPs are identified by the presence of unfolded region due to relatively abundant polar residues content within its amino acid sequence. Together with other residues, IDPs exhibit not only high flexibility but also sensitivity to physico-chemical fluctuation such as pH, temperature, and ions concentration. For this reason, IDPs are involved in cellular processes such as DNA repair scheme and chromatin modification. In this project, we pursue a quantitative description of structure and dynamics of IDPs with different net charges: namely Prothymosin Alpha and Myelin Basic Protein. Here, we employed neutron spin-echo spectroscopy (NSE) and small angle X-ray scattering (SAXS) to gain insight on the emergence of internal friction within the peptide and its conformational change as a function of Guanidinium Chloride (GndCl) concentration respectively. The experimental results obtained from SAXS shows contraction and expansion as measured by FRET. Similarly, from NSE data, we are able to extract the internal friction which is in good agreement with FCS result.