Peer, Laurens (2021) The peculiar asymmetry of the Hsp90 dimer. Bachelor's Thesis, Life Science and Technology.
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Abstract
Since its discovery in 1996, the Hsp90 chaperone has been studied in its role of protein stabilisation in cell stress conditions and in its role of maintaining proteostasis under normal conditions. Abnormalities in its wide variety of clients have been linked to several diseases like cancer, Alzheimer’s disease, and cystic fibrosis. Because of this, the Hsp90 dimer is a prime target for the development of treatments against these diseases. Hsp90 is aided in its functioning by several co-chaperones, but the homodimer is observed to form multiple asymmetric stoichiometries and configurations with its co-chaperones and client proteins. In this thesis three causes of asymmetry in the Hsp90 dimer are explained through the interaction of Hsp90 with three of its co-chaperones: p23, Hop/Sti1, and Aha1. Despite its many client proteins, it should be possible to design treatments with high specificity when using the many ways Hsp90 has developed to interact with its clients.
| Item Type: | Thesis (Bachelor's Thesis) |
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| Supervisor name: | Tych, K.M. and Maglia, G. |
| Degree programme: | Life Science and Technology |
| Thesis type: | Bachelor's Thesis |
| Language: | English |
| Date Deposited: | 13 Aug 2021 10:44 |
| Last Modified: | 13 Aug 2021 10:44 |
| URI: | https://fse.studenttheses.ub.rug.nl/id/eprint/25662 |
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