Proteins are the most complex and versatile molecules that we know. All essential functions of living systems rely at least in part on the actions of proteins. In most cases, proteins are required to be soluble, in order to be functional. However, in many cases, proteins and peptides are observed to undergo liquid-liquid phase separation to enhance their functionality. Often (if not always), phase separated, protein compartments also result in protein aggregation and amyloid fibril formation associated with human diseases. Amyloid fibrils are highly ordered polymeric protein aggregates, and are found in the context of a range of diseases, such as Alzheimer’s and Parkinson’s diseases. It has been proposed that the aggregated state represents the thermodynamically most favorable state of any protein. However, it is not known why that is the case, and how proteins achieve to remain soluble in most cases.
PhD position: Do you want to get trained in a field with a bright future, and ultimately contribute to a more sustainable world? Then join us for a PhD in biophysical studies of plant seed storage proteins, in the framework of the SEEDFOOD project.
- Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation, Emil G. P. Stender, Soumik Ray, Rasmus K. Norrild, Jacob Aunstrup Larsen, Daniel Petersen, Azad Farzadfard, Céline Galvagnion, Henrik Jensen & Alexander K. Buell , Nature Communications, volume 12, Article number: 7289 (2021)
- Mass photometric detection and quantification of nanoscale α-synuclein phase separation, Soumik Ray, Thomas O. Mason, Lars Boyens-Thiele, Nadin Jahnke, Alexander K. Buell, BIORXIV (2022)
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