Within project C11 of the SFB 677 researchers at the Otto-Diels- Institute of Organic Chemistry at the Christian-Albrechts-University, Kiel, aim to modify a naturally occurring antifreeze protein from the fish winter flounder to be able to switch its activity off and on by light. The video describes the background of this proteins, its mechanism of action, and the steps needed to modify it and make its activity light sensitive.
Sönnichsen Group | Christian Albrechts-University of Kiel, Germany
Frank Sönnichsen, Professor in the Otto-Diels-Institute of Organic Chemistry, is a structural biologist and NMR spectroscopist. He has had a long term research interest in a number of protein systems. Among these is the structure function relationship of antifreeze proteins, and the research is aimed at understanding the protein structure and mechanism of action of these unusual proteins.
Hauke Kobarg is a PhD student in the Sönnichsen lab, who synthesizes the modified antifreeze proteins and characterizes the biophysical properties.
Matthias Lipfert is a PhD student in the Sönnichsen lab, who works on a second and novel approach to design a switchable protein module.
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