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.
2020.12.10 | iNano
Associate Professor Victoria Birkedal has received a grant from the Nordisk Foundation with which she will be able to establish Aarhus single molecule fluorescence infrastructure (ASiMoF) for advanced studies of molecular structure, dynamics and function in nano- and bio-systems.
2020.12.03 | iNano
7 iNANO researchers have received between DKK 100,000 and 2,234,000 from the Carlsberg Foundation for specific instruments. The foundation has awarded a total of DKK 67 million for research infrastructure, which aims to strengthen existing research and enable new ideas. In total DKK 6.5 million has been awarded to iNANO researchers.
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)
