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BP: Fachverband Biologische Physik
BP 31: Protein Structure and Dynamics
BP 31.3: Vortrag
Donnerstag, 21. März 2024, 15:30–15:45, H 0112
New insights into the structural dynamics of intrinsically disordered proteins by high-field NMR relaxation experiments — Tobias Stief1,2, Katharina Vormann1,2, and •Nils-Alexander Lakomek1,2 — 1Forschungszentrum Jülich, Structural Biochemistry (IBI-7), 52425 Jülich, Germany — 2Heinrich Heine University Düsseldorf, Institute of Physical Biology, 40225 Düsseldorf Germany
Intrinsically disordered proteins (IDPs) compose about 30% of the human proteome and are highly dynamic entities. Nuclear magnetic resonance (NMR) spectroscopy can provide insights into their structural dynamics at residue-specific resolution. Recently available higher magnetic field strengths, up to 28 Tesla (corresponding to 1.2 GHz 1H Larmor frequency), offer substantially improved resolution, with particular benefits for studying IDPs. We have derived an improved set of 15N NMR relaxation experiments suited for operation at high-field magnets and applicable to fully protonated proteins. Here, we used SNARE proteins as a model system. SNARE proteins play a crucial role during neuronal exocytosis by eliciting the fusion of the synaptic vesicle membrane with the presynaptic plasma membrane. In their pre-fusion state, the membrane-anchored SNARE proteins are disordered. To assess the internal dynamics of the SNARE protein SNAP25, we recorded NMR relaxation experiments at different magnetic field strengths, between 14 and 28T. The field-dependent NMR measurements reveal novel insights into IDP dynamics at the ps-ns timescale.
Keywords: protein dynamics; NMR spectroscopy; relaxation; intrinsically disordered proteins; SNARE proteins