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.
2021.10.15 | iNano
iNANO employees, Professors Jeppe Vang Lauritsen and Duncan Sutherland, and iNANO member, Professor Mogens Christensen, receive fundings from the Independent Research Fund Denmark. The researchers will study electrocatalytic hydrogen production, materials for building solar-thermal management, and compaction of Magnets, respectively.
2021.10.12 | iNano
The use of solid-state NMR spectroscopy is pivotal in enabling the characterisation of structure and dynamics at the atomic-level. These methods rely on access to sophisticated and costly solid-state NMR equipment that is only available in few national facilities. The Danish Center for Ultrahigh Field NMR Spectroscopy at Aarhus University, with…
2021.10.07 | iNano
In a collaborative effort with Professor Birgit Schiøtt (iNANO member) and her research group, the researchers also used state-of-the-art Molecular Dynamics simulations to support the notion of proton binding employing multiple independent approaches.
