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Protein Biophysics (Prof. Daniel Otzen)

Daniel Otzen

Professor Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset
Group members
Research funding

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.  

News

Using gadolinium (contrast agent used in MRI scans) may revolutionize the application of Nuclear Magnetic Resonance spectroscopy as a tool for more comprehensive and useful analysis of urine samples (Image: Colourbox.) 
A proton NMR spectrum. Signals are due to different metabolites, with their peak integrals equal to their amount. Along the y-axis the T1 recovery time constant for each peak in the absence (red) and presence (blue) of adjuvant. This means that the lower T1, the faster the recording. (Graphics by Frans Mulder.)

2019.08.21 | iNano

New efficient method for urine analysis may tell us more

Our urine reveals our well-being and how we treat our body. A researcher at Aarhus University has developed an effective method of analysis for examining the constituents of a urine sample, using contrast agent, as a cost-effective adjuvant. This can have a major impact on future healthcare.

On the raw electron micrographs (A), one can find the individual protein molecules (green boxes). By taking an average of thousands of such similarly oriented particles, one can get sharp two-dimensional images (B), from which one can calculate the protein's three-dimensional structure (C). Finally, one can interpret this result by building a model of the protein (D). Image: Milena Timcenko.

2019.06.27 | iNano

Groundbreaking cryo-electron microscopy at Aarhus University reveals the first structures of a protein that maintains cell membranes

Using cutting-edge electron microscopy, researchers from Aarhus University have determined the first structures of a lipid-flippase. The discoveries provide a better understanding of the basics of how cells work and stay healthy, and can eventually increase our knowledge of neurodegenerative diseases such as Alzheimer’s.

Marianne Glasius participates in programme, funded by the Novo Nordisk Foundation, for developing more productive crops. (Photo by Lars Kruse, AU Photo)

2019.06.18 | iNano

An international research team receives EUR 27 million to develop more productive crops

The Novo Nordisk Foundation awards EUR 27 milllion to the Collaborative Crop Resilience Programme (CCRP). The programme will investigate the interaction between roots and leaves with bacteria and help reduce the use of fertilizers. Assoc. Prof. Marianne Glasius is participating in one of the programmes, InRoot.

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