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.
2020.09.09 | iNano
The research initiative LifeTime represents more than 50 European universities, including Aarhus University. A new Perspective article in Nature, co-authored by Jørgen Kjems from iNANO and Department of Molecular Biology and Genetics, outlines LifeTime's vision of how to revolutionize healthcare through personalised, cell-based interceptive…
2020.09.08 | iNano
Structural disorder is vital for proteins’ function in diverse biological processes. It is therefore highly desirable to be able to predict the degree of order and disorder from amino acid sequence. AU researchers have developed a prediction tool by using machine learning together with experimental NMR data for hundreds of proteins, which is…
2020.09.03 | iNano
Congratulations to Peter Balling, who per. 1 September 2020 has been appointed professor of experimental physics at the Department of Physics and Astronomy at Aarhus University.
