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BP: Fachverband Biologische Physik
BP 17: Protein Structure and Dynamics
BP 17.4: Talk
Wednesday, March 29, 2023, 15:45–16:00, BAR 0106
Structural dynamics of the intrinsically disordered SNARE proteins at the membrane interface: Recent insights by NMR spectroscopy — Tobias Stief1,2, Mirko Kraus1,2, Katharina Vormann1,2, Reinhard Jahn3, Angel Perez-Lara4, and •Nils-Alexander Lakomek1,2 — 1Forschungszentrum Jülich, Jülich, Germany — 2Heinrich-Heine-Universität, Düsseldorf, Germany — 3Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany — 4University of Granada, Granada, Spain
SNARE proteins play a crucial role during neurotransmitter release by eliciting the fusion of the synaptic vesicle membrane with the presynaptic plasma membrane. In their pre-fusion state, the SNARE proteins are intrinsically disordered. They do not exhibit a well-defined structure and show high internal flexibility, being membrane-anchored. However, the mode of interaction between the SNARE proteins and the lipid membrane needs to be better understood.
We use the SNARE proteins as a model system for developing novel NMR methods to characterize the inner and conformational dynamics of intrinsically disordered proteins interacting with lipid membranes or being membrane-anchored. Therefore, we address a large range of timescales, from pico- to milliseconds, employing both solution NMR and solid-state NMR methods. The aim is to better describe the conformational space of intrinsically disordered proteins at the lipid membrane interface. At the conference, we will present recent (unpublished) insights into the structural dynamics of the SNARE protein synaptobrevin-2 at the lipid membrane interface.