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.
2020.09.25 | iNano
The properties of nanoparticles are widely acknowledged and they are an important tool in pharmaceutical applications, among others. However, there is a need for deeper understanding of the protein layers accumulating on their surface, as these protein layers affect the functional role of the nanoparticles. AU researchers have developed a method…
2020.09.21 | iNano
A so-called circular RNA molecule, which is thought to be carcinogenic, is not present in cancer cells after all. A Danish research team has published the new results in Nature Communications.
2020.09.18 | iNano
Cryogenic Electron Microscopy (cryo-EM) has become a truly important technique in molecular cell biology as well as medicine and biotechnology. Together with the University of Copenhagen, Aarhus University has established state-of-the-art cryo-EM facilities in Aarhus and Copenhagen, which will be inaugurated on October 12, 2020. The research…
