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.
2020.06.25 | iNano
A new paper from Jørgen Kjems' group at iNANO and MBG describes how expression of non-coding RNA changes during epileptic seizures in rodents. The authors found that inhibiting a specific set of microRNAs (miRNAs) by antisense technology reduced seizure frequency in a mouse model, suggesting that these RNA molecules could serve as possible targets…
2020.06.15 | iNano
An international research team has used new X-ray techniques to describe how the architecture of healthy human bones is built up. The team has uncovered a hitherto unknown structure in healthy bones.
2020.05.29 | iNano
Daniel Otzen and collaborators, Jørgen Kjems and Victoria Birkedal from the Interdisciplinary Nanoscience Center (iNANO) and the company Fida Biosystems, have received DKK 3.8 million from the Innovation Fund Denmark to develop a screening system to identify drugs that are able to combat COVID-19.
