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.
2019.12.13 | iNano
A scientific collaboration led by researchers at iNANO/Department of Molecular Biology and Genetics at Aarhus University and the Department of Chemistry at the University of Copenhagen has resulted in the construction of a synthetic DNA nanopore capable of selectively translocating protein-size macromolecules across lipid bilayers.
2019.12.10 | iNano
The Lundbeck Foundation is awarding grants worth DKK 232 million (USD 34 million) to six leading neuroscientists. The LF Professorships programme is the Foundation’s largest grant allocation to date.
2019.12.05 | CADIAC
Assist. Prof. Xinming Hu and Prof. Kim Daasbjerg from Carbon Dioxide Axtivation Center (CADIAC) at Aarhus University describe the state-of-the-art of the electrochemical CO2 reduction promoted by molecular catalysts and discuss an important recent discovery published in Nature. Read the Nature News & Views article by Hu and Daasbjerg here.
