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.
2019.06.27 | iNano
Using cutting-edge electron microscopy, researchers from Aarhus University have determined the first structures of a lipid-flippase. The discoveries provide a better understanding of the basics of how cells work and stay healthy, and can eventually increase our knowledge of neurodegenerative diseases such as Alzheimer’s.
2019.06.18 | iNano
The Novo Nordisk Foundation awards EUR 27 milllion to the Collaborative Crop Resilience Programme (CCRP). The programme will investigate the interaction between roots and leaves with bacteria and help reduce the use of fertilizers. Assoc. Prof. Marianne Glasius is participating in one of the programmes, InRoot.
2019.06.14 | iNano
Researchers at Aarhus University are developing new chemical technologies to reduce CO2 emissions and support the green transition in both public and private manufacturing companies.
