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| Art des Jobs | Vollzeit | |
| Eingetragen am | 11.04.2024 | |
| Einsatzort | München | |
| Jobbeschreibung | General description Membraneless organelles (such as nucleoli, nuclear speckles, stress granules etc.) are vital for living organisms. These biomolecular condensates are formed by multi-domain proteins that are involved in multi-valent interactions. Condensate formation implies both protein-protein and protein-RNA interactions, involving prion-like low complexity regions and RNA binding domains. The delicate balance between liquid-liquid phase separation (LLPS) and amyloid fibril formation requires tight regulation. This can be achieved by chaperones, posttranslational modifications, small molecules and/or metals that affect this balance and either yield disintegration or rigidification of protein liquid droplets into ?-strand rich protein fibrils. It is the aim of the PhD project to better understand the mechanisms that modulate the equilibrium between amyloid fibril and granule formation in the cell on a structural basis. Protein systems under investigation involve stress granule (SG) associated factors, the Alzheimer’s disease A? peptide, the diabetes type II related human islet amyloid polypeptide (hIAPP/amylin), light chain antibody domains involved in AL-amyloidosis and serum amyloid A (SAA) involved in AA-amyloidosis. We employ solution- and MAS solid-state NMR to characterize these systems. In addition, we use low resolution biophysical methods such as fluorescence microscopy, ThT aggregation assays, CD spectroscopy, electron microscopy and dynamic light scattering (DLS). |
| Qualifikationen | Interested candidates should have a strong background in biochemistry and biophysical methods to characterize protein misfolding. |
| Firma |
Technische Universität München (TUM) 80333 München |
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