Structure and dynamics are usually what determines the function of a protein in the cell. Even though one of the two can sometimes play a more important role than the other, or only a transient structure is formed in the course of protein interactions, only the combination of both provides a faithful representation of the molecular behavior. Nuclear Magnetic Resonance (NMR) spectroscopy is able to deliver information on both such parameters in a range of molecular sizes and dynamics time scales. Structural information is obtained by a characterization of chemical shifts, interatomic distances, and the size and direction of other interactions, whereas dynamics are mostly represented by the lifetimes of different non-equilibrium states in addition to internuclear interactions. The Linser group develops and uses state-of-the-art NMR spectroscopic tools for the understanding of protein structural and dynamic features that govern their functionality. We employ both, solid-state NMR as well as solution NMR spectroscopy, both in terms of method development and applications. One of our major foci is to use the rich information content of protons for solid-state NMR purposes, i. e. unambiguous resonance assignment, protein structure, and protein dynamics, but there are many more topics of interest, and many more ways in which NMR can solve biological questions. We just moved to Munich from the Max Planck Institute for Biophysical Chemistry, Göttingen. As we are still expanding our group, predominantly in the direction of solution NMR, please do not hesitate to contact us for current opportunities to join the team.