ESR6: Top-down paleoproteomics. (@ UCPH, supervisor JVO).
As an alternative to bottom-up proteomics, the emergence of new ion dissociation methods continues to drive top-down proteomics by offering valuable alternatives to traditional slow-heating methods (e.g., collision-activated dissociation, CAD). Electron transfer dissociation (ETD) leverages electron-driven radical rearrangements to promote cleavage of N–Cα bonds between amino acid residues, preserving labile post-translational modifications (PTMs) and providing extensive sequence-informative fragmentation of peptides and proteins. The complementary of the different types of fragmentation methods significantly increases confidence in peptide and protein identification in particular for PTM analyses. Therefore, top-down analysis allows for the measurement of intact protein masses and provides information on post-translational modifications, as well as the protein sequence via fragmentation of the intact proteins in the mass spectrometer. Application of top-down proteomics to cultural heritage materials will remove many of the limits hampering analysis of this category of samples.
Networking. Within TEMPERA, ESR 6 will interact primarily with:
- ESR 7: ESR 6 will spend a secondment period of 6 months at MPI (co-supervision) to collaborate with ESR 7 and colleagues for automatic interpretation of the data he/she will generate using the methodologies he/she will develop.
- ESR 8: ESR 6 will spend a secondment period of 6 months at Thermo (Bremen) to work on hardware improvement in a company environment.
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🇪🇺 This project has received funding from the European Union's EU Framework Programme for Research and Innovation Horizon 2020 under Grant Agreement No. 722606. 🇪🇺