The research of the solid-state NMR group led by Prof. Beat Meier and Prof. Matthias Ernst is centered on solid-state NMR structure determination of biomolecules (fibrils, membrane proteins, protein-DNA complexes) and NMR method development. The detection of protein-DNA interactions is a central line of research (project leader Dr. Thomas Wiegand) and is the prerequisite for understanding molecular details of DNA replication. We are seeking applications for a
PhD position - Magnetic-resonance approaches to study protein-DNA interactions in motor proteins
The project will focus on the development of MAS (magic-angle spinning) NMR spectroscopy approaches to characterize protein-DNA interactions. The bacterial DnaB helicase from Helicobacter pylori serves as the model system and the student will investigate the interplay between dynamics, structures and functions of several arrested states of the ATP-hydrolysis and DNA-binding reaction coordinate. Protein-protein interactions will be probed in the primosome which is the complex of the helicase with a primase. A whole variety of techniques will be applied, e.g. heteronuclear correlation experiments (31P/13C, 1H/31P), 1H-detected MAS spectroscopy at MAS frequencies > 111 kHz, paramagnetic NMR employing paramagnetically labelled DNA, MAS-Dynamic Nuclear Polarization (DNP) to enhance the nuclear polarization, Electron Paramagnetic Resonance (EPR) spectroscopy.
Prerequisites are a Master in Chemistry, Biochemistry, Physics, Interdisciplinary Sciences, or related areas. The successful candidate should have a strong interest in spectroscopic techniques and in their applications to biomacromolecules. Basic experience in NMR is beneficial. Interest in practical work in the biochemistry laboratory is expected, since the student will prepare the biological samples in collaboration with a technician.