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.
News Highlights
Congratulations Alex on receiving an 2 M Euro European Research Council (ERC) Consolidator grant for his project “Exploring the molecular grammar of IDP assembly and condensation at ultra-high throughput” with the acronym EMMA.
Important Publications
- 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)
- Ray, S., Mason, T.O., Boyens-Thiele, L. et al. Mass photometric detection and quantification of nanoscale α-synuclein phase separation. Nature Chemistry. 15, 1306–1316 (2023). https://doi.org/10.1038/s41557-023-01244-8
Highlights of the instruments/facilities we provide:
Refeyn Two MP, In-house microscopy, FIDA1, OpenTrons robotics, microfluidics fabrication facility, Prometheus PANTA DLS, Labbot and many more biophysical tools.
We are a group of interdisciplinary scientists exploring brand new avenues of protein science. We provide an outstanding research environment equipped with state-of-the-art facilities and beyond. Highly motivated young minds from across the globe provides an international environment enriched in knowledge as well as culture.
Location
DTU Bioengineering
Building 227
Technical University of Denmark
Søltofts Plads
2800 Kgs. Lyngby
Protein Biophysics at DTU Bioengineering 