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.
2020.09.03 | iNano
Congratulations to Peter Balling, who per. 1 September 2020 has been appointed professor of experimental physics at the Department of Physics and Astronomy at Aarhus University.
2020.09.01 | iNano
New results, with implications for catalysis used for cleaning up crude and bio oils, show that a reactant molecule can generate its own larger active site, when it is adsorbed onto certain vacancy positions on MoS2 nanoparticles. The finding has been published in Nature Communications by the group of Jeppe V. Lauritsen at iNANO, Aarhus University.
2020.08.21 | iNano
Congratulations to Jakob B. Grinderslev who received this year's Danscatt PhD award for his PhD thesis about his work within boron and nitrogen based complex metal hydrides as energy storage materials.
