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.
2020.09.18 | iNano
The Novo Nordisk Foundation has granted DKK 15 million from its interdisciplinary synergy programme to project DRAMA. With researchers from both Nat and Tech, including Merete Bilde and Tobias Weidner, the project will decipher the role of atmospheric microbial aerosols for cloud formation.
2020.09.18 | iNano
Skrydstrup Group has developed a simple, secure, and highly efficient protocol for producing aldehydes, which are important chemical building blocks. The method includes using their two-chamber reactor, and the results have been published in the highly renowned journal, Nature Catalysis. The synthetic methodology is foreseen to have an impact for…
2020.09.15 | iNano
VILLUM Experiment has just awarded grants to Danish researchers, who each represent innovative approaches to their research areas, and thus to test their brave and strange technical and scientific research ideas. Associate Professor Alexander Zelikin and Professor Kim Daasbjerg are among the recipients.