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.
2020.05.13 | iNano
Ever wondered if you could see through the body of a living organism and observe the dynamic interplay between cells and nanoparticles injected into the bloodstream? Pia Bombolt and Thomas Boesen contribute to research published in ACS Nano showing how the use of transgenic zebrafish embryos now offers a unique opportunity for intravital…
2020.04.24 | iNano
The healthcare system and the economy are under pressure in many parts of the world due to the ongoing COVID-19 pandemic. With fundings from Independent Research Fund Denmark Professor Jørgen Kjems will, in collaboration with researchers from DTU and Rigshospitalet, develop a method that can detect the virus at very early stages of infection and,…
2020.04.24 | iNano
Associate Professor Alexander Zelikin and his research team publish in Angewandte Chemie Int. Ed. on new results which makes tumor‐targeted glucuronides attractive for translational medicine.
