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.
2019.12.05 | 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.
2019.11.29 | iNano
The discovery of a unique technology to detect small molecules in blood, and the potential of being able to secure a more correct and safe treatment of certain patients, led iNANO researchers to establish the startup company, MedicQuant. The team behind the company has just won the Bioinnovation Institute (BII) Acceleration Award.
2019.11.28 | iNano
A total of DKK 11,7 million have been awarded by the Carlsberg Foundation to researchers currently or formerly affiliated with Interdisciplinary Nanoscience Center (iNANO) at Aarhus University.