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.
2020.01.20 | iNano
13 iNANO associated researchers have been granted DKK 8 million from the Carlsberg Foundation for research infrastructure
2019.12.20 | iNano
Henrik Birkedal, Merete Bilde, Tobias Weidner, Thomas Boesen, Rikke Louise Meyer, and Alexander Zelikin receive DKK 36 million in total from the Novo Nordisk Foundation for infrastructure for studying bone structure, studies in microbial aerosols, and the battle against antimicrobial resistance.
2019.12.19 | iNano
Professor Troels Skrydstrup has been interviewed by Chemistry Views (Wiley) about his successful work in organic synthesis, organometallic chemistry, and especially running safe reactions with dangerous but very useful gases, like carbon monoxide and hydrogen cyanide. Hear about his research plans and why Denmark is a nice place to do research.
