Dresden 2020 – wissenschaftliches Programm
Die DPG-Frühjahrstagung in Dresden musste abgesagt werden! Lesen Sie mehr ...
Bereiche | Tage | Auswahl | Suche | Aktualisierungen | Downloads | Hilfe
BP: Fachverband Biologische Physik
BP 17: Poster V
BP 17.9: Poster
Dienstag, 17. März 2020, 14:00–16:00, P2/1OG
Structural Dynamics Correlation of Peptides derived from Nucleoporins: Time-resolved X-ray Scattering and Computational Modelling — •Naireeta Biswas1 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
Nuclear pore complexes (NPCs) form aqueous conduits along the nuclear membrane, controlling exchange of macromolecules between the cytoplasm and the cell nucleus is built up of ~ 30 different types of proteins called as nucleoporins(Nups) which contain phenylalanine-glycine (FG) repeating motifs know as FG repeat domains. FG repeat domains are intrinsically disordered. The FG domains facilitate a highly selective, bidirectional passage of macromolecules through the NPCs thus forming the permeability barrier. Several models for the highly selective nature of the permeability barrier of the NPCs have been proposed. According to the selective phase model, the NPC permeability barrier is constructed through cohesive meshwork of the FG domains by weak hydrophobic interactions between the phenylalanine residues forming a sieve like 3D hydrogel within the central channel of the NPCs.
To get an insight in the structural dynamics of these FG Nups, we are investigating the molecular dynamics of the FG repeat domains and their interactions during the gelation process using time-resolved small/wide-angel X-ray scattering (TR-SAXS/WAXS) techniques and molecular dynamics simulation.