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.
2019.10.11 | iNano
Partial unfolding of proteins can be a big problem in industry, as it may affect the stability of products. So how does an empty space or cavity in its hydrophobic core destabilize a protein? And would such a cavity in fact be empty? These are some of the questions researchers from Aarhus University answer in a new study.
2019.10.09 | iNano
PhD student in Associate Professor Henrik Birkedals research group receives poster prize at the European Synchrotron Radiation Facility
2019.10.08 | iNano
Congratulations to Nanoscience student Malthe von Tangen Sivertsen, who is the first student to have completed the challenge program in nanoscience at Interdisciplinary Nanoscience Center, Aarhus University.
