The liquid-liquid phase separation (LLPS) of biomolecules is a phenomenon which received a lot of attention in the last years because it is not only related to theformation of membraneless organelles but also to neurodegenerative diseases. Lysozyme is a globular protein that undergoes LLPS in a buffer salt system andfor that it is well investigated with several techniques like microscopy, dynamic lightscattering (DLS) or small-angle X-ray scattering. In this work we investigate the effect of temperature, solvent and sample con-centration on the diffusion coefficient, the hydrodynamic radius and the viscosity oflysozyme using a DLS setup. Furthermore, the influence of these parameters on thecluster formation is addressed. Finally, we investigate the question if the LLPS oflysozyme in a buffer environment effects the formation of dynamic clusters.
| Identifer | oai:union.ndltd.org:UPSALLA1/oai:DiVA.org:su-193168 |
| Date | January 2021 |
| Creators | Poggemann, Hanna-Friederike |
| Publisher | Stockholms universitet, Fysikum |
| Source Sets | DiVA Archive at Upsalla University |
| Language | English |
| Detected Language | English |
| Type | Student thesis, info:eu-repo/semantics/bachelorThesis, text |
| Format | application/pdf |
| Rights | info:eu-repo/semantics/openAccess |
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