Patterns of protein stability and interactions in water-cosolvent systems
- The basis of the present study represents the aim in bringing a contribution to the elucidation of certain thermodynamic and molecular aspects characterizing protein-cosolvent and protein-protein interactions and how these two types of interactions are interrelated. The investigation of protein-cosolvent systems was mainly based on ionic species and, in particular, on a special class of organic salts known under the general name of "ionic liquids". By investigating a multitude of ionic liquids, it was possible to rank them in a Hofmeister series, based on the extent of stabilizing/destabilizing effect on the proteins. More, the ionic liquids show the capacity to prevent protein aggregation. The unfolding - dissociation mechanism and the thermodynamic equilibrium between the oligomerization domains of MST1 and Nore1 (the SARAH domains) - having a role in the Ras-induced apoptosis pathway was also investigated.
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| Author: | Diana Constantinescu AruxandeiGND |
|---|---|
| URN: | urn:nbn:de:hbz:294-28786 |
| Referee: | Christian HerrmannORCiDGND, Hermann WeingärtnerGND |
| Document Type: | Doctoral Thesis |
| Language: | English |
| Date of Publication (online): | 2010/09/20 |
| Date of first Publication: | 2010/09/20 |
| Publishing Institution: | Ruhr-Universität Bochum, Universitätsbibliothek |
| Granting Institution: | Ruhr-Universität Bochum, Fakultät für Chemie und Biochemie |
| Date of final exam: | 2010/04/29 |
| Creating Corporation: | Fakultät für Chemie und Biochemie |
| GND-Keyword: | Thermodynamik; Proteine; Lösungsmittel; Oligomerisation; Apoptosis |
| Dewey Decimal Classification: | Naturwissenschaften und Mathematik / Chemie, Kristallographie, Mineralogie |
| faculties: | Fakultät für Chemie und Biochemie |
| Licence (German): |  Keine Creative Commons Lizenz - es gelten der Veröffentlichungsvertrag und das deutsche Urheberrecht |
