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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

CADIAC publishes in Journal of the American Chemical Society on a novel approach to isotopically labeled beta-amino acid /beta-aminoketone fragments. Image: Reprinted and modified with permission from J. Am. Chem. Soc.20191413011821-11826. Copyright 2019 American Chemical Society.

2019.09.05 | iNano

New synthetic technique for carbon isotope labeling

CADIAC publishes in Journal of the American Chemical Society where they report on a novel method for the introduction of carbon isotopes into pharmaceutical relevant molecules.

Associate Professor Rikke Louise Meyer receives ST Industrial Collaboration Award 2019. (Photo: Lars Kruse, AU Photo)

2019.08.26 | iNano

ST Award goes to iNANO researcher

Congratulations to Associate Professor Rikke Louise Meyer (iNANO and Dept. of Bioscience) who has received this year's Industrial Collaboration Award given by Science and Technology, Aarhus University's faculty of science and technology.

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.

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