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.
2020.04.03 | iNano
Working and studying has been different in just as many ways as there are employees and students, and together, each in their own way, they are keeping the wheels of NAT running. Separately. Meet some of them here, including Daniel Dupont at iNANO.
2020.04.01 | iNano
Professor Birgit Schiøtt (Department of Chemistry and iNANO) has received a VILLUM Synergy grant of DKK 3.0 million together with Professor Ira Assent (Department of Computer Science) for development of new cluster models that can provide a more accurate insight into proteins at the molecular level.
2020.03.25 | iNano
The demand for energy is growing and so is the demand for alternative energy solutions, which includes living sources of electricity. AU researchers have in collaboration with an international team created microbial energy cells and shows a method for improving the efficiency of bioelectrical systems.
