Our research activities fall within 3 main areas, which all relate to the study of the kinetics and thermodynamics of protein conformational changes, namely membrane protein folding, protein-detergent interactions and protein fibrillation. These areas are linked by a keen interest in understanding the mechanistic and thermodynamic behaviour of proteins in different circumstances by quantifying the strength of internal side-chain interactions as well as contacts with solvent molecules, whether it be detergents, denaturants, stabilizing salts and osmolytes or lipids. Ultimately we hope this will lead to a greater manipulative ability vis-a-vis processes of both basic, pharmaceutical and industrial relevance. The general approach is to use available spectroscopic techniques (fluorescence, CD, stopped-flow, FTIR, NMR and dynamic and static light scattering) to generate data which can be analyzed in a quantitative manner to develop models and mechanisms for conformational changes at the molecular level.
2020.11.25 | iNano
Listen to Henrik Birkedal and Mads Ry Jørgensen tell about DanMax, a materials science beamline at MAX IV accelerator in Lund. Learn both how high-energy X-rays are made, how X-rays must be treated before you can use it, and not least what Danish researchers hope to be able to use the expensive device for. (In Danish)
2020.11.20 | iNano
New findings by Professor Daniel Otzen and his research team show that baicalein, a traditional Chinese medicine, incorporated in nanoliposomes may protect against the destructive attacks by alpha-synuclein, which is the cause of Parkinson's disease. Read about the findings here on sciencenews.dk.
2020.11.20 | iNano
Researchers from Aarhus University look forward to building bridges with Japanese and Israeli researchers within molecular science, biomolecular design, and artificial biology. With grants from the Ministry of Education and Research, activities can be established that can kick-start the budding research collaboration across continents.
