Characterization of conformational dynamics in proteins and their interaction partners by solid-state NMR spectroscopy (A13#)

• Subject Area: Physical Chemistry of Molecules, Liquids and Interfaces, Biophysical Chemistry
• Term: from 2017 to 2019
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 27112786

In this work we plan to develop and employ new solid-state NMR approaches that make use of the potential of protons as sensitive reporters for dynamic processes in proteins. Besides the quantitative tailoring of these methods on model systems the arising possibilities will be exploited for two biologically important topics. On one hand, this concerns the interactions of a secondary messenger with a protein interaction partner. On the other, we will use these methods to quantify the dynamic interactions between water and the active site of an enzyme.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 749: Dynamics and Intermediates of Molecular Transformations
• Applicant Institution: Ludwig-Maximilians-Universität München
• Project Head: Professor Rasmus Linser, Ph.D.