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Tau conformational changes induced by phosphorylation and 14-3-3 proteins relevant in neurodegenerative diseases


Project Description

The main neuropatological signs of Alzheimer disease are associated with the fibrillization of tau protein into neurofibrillar tangles. Studying of how different factors influence the formation of protein fibrils is the key for understanding these neurodegerative processes. The main aim of this PhD project will be characterization of conformational changes in the formation of tau fibrils due to their truncations, phosphorylation and the interaction with 14-3-3 proteins. Interdisciplinary approach combining biomolecular NMR, biophysical interaction techniques and computational methods will be applied. The described activities are part of international research projects allowing to spend the part of PhD study at the groups of our collaborators in Europe or North and South America and to learn specific research techniques, there.

Keywords: Molecular Biophysics, tau protein, phosphorylation, 14-3-3 proteins, neurodegenerative diseases, NMR, computational simulations

HOW TO APPLY: Register for this call using the registration form at http://ls-phd.ceitec.cz/http-ls-phd-ceitec-cz/ and submit required documents to receive support with the preparation of the application and all formalities. Your application package will be forwarded to the supervisor for preliminary revision.
Applicants who wish to pursue a degree at the CEITEC PhD program must hold the equivalent of a Master’s degree (MSc) in similar field (four- or five-year undergraduate degree). The application can be submitted before obtaining the Master’s degree, however, the applicant should obtain the degree within five months after the application deadline.

Funding Notes

Admission for studies, student registration for the full-time study program and proper fulfilment of student duties constitute the student’s right to a regular income of 22 000 CZK (850 EUR). Information is available at View Website

Living costs and other practicalities available at View Website

References

1. Lippens, G., and Gigant, B. Elucidating Tau function and dysfunction in the era of cryo-EM. J. Biol. Chem. 2019, 294, 9316–9325.
2. Přecechtělová, J.; Mládek, A.; Zapletal, V.; Hritz, J.: Quantum Chemical Calculations of NMR Chemical Shifts in Phosphorylated Intrinsically Disordered Proteins, JCTC 2019, 15, 5642-5658.
3. Melková, K.; Zapletal, V.; Jansen, S.; Nomilner, E.; Zachrdla, M.; Hritz, J.; Novácek, J.; Zweckstetter, M.; Ringkjøbing-Jensen, M.; Blackledge, M. and Žídek, L.: Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics. J. Biol. Chem. 2018, 293, 13297-13309.
4. Nagy, G., Oostenbrink, C., and Hritz, J. Exploring the binding pathways of the 14-3-3ζ protein: Structural and free-energy profiles revealed by Hamiltonian replica exchange molecular dynamics with distancefield distance restraints. PLoS One 2017, 12, 1–30.
5. Motáčková, V., Nováček, J., Zawadzka-Kazimierczuk, A., Kazimierczuk, K., Žídek, L., Šanderová, H., Krásný, L., Koźmiński, W., and Sklenář, V. Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced 5D experiments. J. Biomol. NMR 2010, 48, 169–177.

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