BPCPPDYSOE21 – scientific programme
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BP: Fachverband Biologische Physik
BP 11: Poster A: Single Molecule, Multicellular, Bioimaging, Focus Sessions, etc.
BP 11.8: Poster
Monday, March 22, 2021, 16:30–19:00, BPp
Structural Dynamics Correlation of Peptides derived from Nucleoporins: Time-resolved X-ray Scattering and Computational Modelling — •Naireeta Biswas1,2, Markus Osterhoff2, Jakob Soltau2, Sheung Chun Ng3, Dirk Görlich3, and Simone Techert1,2 — 1FS-SCS, Deutsches Elektronen-Synchrotron (DESY), Notkestraβe 85, 22607 Hamburg, Germany — 2University of Göttingen, Institute for X-ray Physics, Friedrich-Hund-Platz 1, 37077 Göttingen, Germany — 3Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany
FG nucleoporins are intrinsically disordered proteins located in the nuclear pore complexes (NPCs) consist of FG repeating motifs. It has been proposed that repeating motifs play an important role in the formation of hydrogel due to their cohesive interactions and hydrophobic nature. These protein hydrogels show unique features of non-covalent interactions such as hydrogen bonding, Vander Waals interaction or π-π stacking, driving the protein self-assembly, leading to an anisotropic structural growth, thus forming hydrogels with unusual materials properties. Our computational simulations, suggest different conformations and interactions between these FG repeating motifs and that these conformational variety may be the driving forces for the co-existing domains. To understand this molecular rationale of the protein kinetics during their gelation process, we have studied the first steps of self-assembling and structural organization of the protein hydrogels during the formation .