University of Twente Student Theses
Chain dynamics as a measure for internal friction in the intrinsically disordered protein alpha-synuclein
Boamfa, Anamaria (2022) Chain dynamics as a measure for internal friction in the intrinsically disordered protein alpha-synuclein.
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| Abstract: | Intrinsically disordered proteins (IDPs) are proteins that lack a fixed three-dimensional structure, there is no folding of the protein into a secondary or tertiary structure. In general, IDPs have a dynamic conformation flexibility, meaning that their shape changes over time. The conformational dynamics of IDPs are still poorly understood. The protein alpha-synuclein (αS) is an IDP that is linked to neurodegenerative diseases such as Parkinson’s and dementia with Lewy bodies. It is known that many mechanisms are of influence on the aggregation behaviour of αS, however, the exact cause or trigger that originates the formation of αS aggregates is not yet clearly understood. One factor of influence is the change in conformational dynamics of the protein due to environmental factors. This thesis aims to obtain more fundamental insight into the chain dynamics of αS monomers, in order to get a better understanding of the protein and its aggregation behaviour. The dynamics of αS are investigated with nanosecond Fluorescence Correlation Spectroscopy (nsFCS) in combination with single-molecule Forster Resonance Energy Transfer (smFRET). With these techniques, the reconfiguration time of the protein is determined for the N-terminus, NAC region and the C-terminus of the protein.The reconfiguration time is used to study the conformation dynamics of the protein and its change in different solvents. |
| Item Type: | Essay (Master) |
| Faculty: | TNW: Science and Technology |
| Subject: | 02 science and culture in general, 33 physics, 42 biology |
| Programme: | Biomedical Engineering MSc (66226) |
| Link to this item: | https://purl.utwente.nl/essays/92023 |
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