In this work the structure, dynamics and interactions of proteins were investigated by using nuclear magnetic resonance spectroscopy (NMR) and other techniques. By a combination of NMR and other biophysical methods the solution structure and the essential function of the non-repetitive domain of a spider silk protein could be determined. Furthermore, the dynamics and interaction with partner proteins, substrates and ligands in the Hsp90 chaperone system was a central part of this work. For another heat shock protein, Hsp12, structure, dynamics and membrane location could be determined. Another part of this work is the investigation of the interaction between BclxL and the tumorsuppressor protein p53. This interaction plays a crucial role for the induction of apoptosis. With these data, a model of the action of p53 at the mitochondria could be postulated. Furthermore, screening for new p53-stabilizing molecules was done and the binding site of the best compounds could be determined. The method of choice was NMR but also biochemical and other biophysical methods have been used.
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In this work the structure, dynamics and interactions of proteins were investigated by using nuclear magnetic resonance spectroscopy (NMR) and other techniques. By a combination of NMR and other biophysical methods the solution structure and the essential function of the non-repetitive domain of a spider silk protein could be determined. Furthermore, the dynamics and interaction with partner proteins, substrates and ligands in the Hsp90 chaperone system was a central part of this work. For anot...
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