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.
2020.03.11 | iNano
Aarhus University and a number of international pharmaceutical manufacturers are joining forces in a groundbreaking, open research collaboration, ODIN (Open Discovery Innovation Network), which the Novo Nordisk Foundation supports with DKK 54.5 million. Data and results from the collaboration are made open and free to the outside world. The…
2020.03.06 | iNano
Converting CO2 into more useful products offers an interesting strategy to mitigate climate issues while producing value added chemicals. Researchers from the Carbon Dioxide Activation Center (CADIAC) have discovered how the ligand scaffold around a manganese catalyst can be modified to control the selectivity of the products generated via…
2020.02.28 | iNano
Carbon isotope labeling of new drug candidates is an important process for allowing preclinical and clinical investigations on a specific compound’s distribution, metabolism, and toxicity. AU researchers have found a new method for this with broad applicability.
