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Protein Biophysics (Prof. Daniel Otzen)

Daniel Otzen

Professor Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset

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Research focus in brief

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.  

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News

Easy and inexpensive method for linking other molecules to DNA sequences with desired functions

Professor Kurt Gothelf and Ph.D. Angel Santorelli. (Photo: Aarhus University)

The development of new types of drugs based on DNA and RNA is happening at a rapid pace. The mRNA vaccines against COVID-19 are just one of many examples of DNA-based drugs on the market. Many are on the way, but the production of the necessary DNA is costly.

A research group at Aarhus University has now found an effective and inexpensive method for producing stable DNA sequences attached to chemical groups that e.g., ensures that the drugs are directed into the right cells.

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