Structural biology is concerned with elucidation of biomolecules, in particular proteins, with respect to their atomic-resolution 3D structures, dynamics, and interactions with other molecules in order to shine light on the principles behind their physiological functionality. As such, the related research yields a detailed understanding of the mechanisms constituting cellular life and the possibilities of medical treatment to interfere with any aberrant or mis-regulated processes. In particular, the dynamics of proteins, happening on manifold timescales from ps to ms, represent a feature that has been difficult to grasp but constitutively important for the individual proteins' functionality.
Nuclear Magnetic Resonance (NMR) spectroscopy is based on the interaction of nuclear magnetic momenta with an external magnetic field and the readout of resonance frequencies, lifetimes of non-equilibrium states, and spatial spin proximities. Employing such principles, the technique is capable of assessing molecular structure and dynamics with of atomic resolution. This can be applied to proteins: Soluble proteins can be characterized using a huge set of established solution NMR methodology. On the other hand, solid-state NMR is applied for example to study membrane proteins in a lipid-bilayer setting or amyloidogenic proteins. This approach has witnessed significant developments in the strategies employed in the last years. One such development is the availability of proton detection rather than detection of heteronuclear signals, which has been driven by the methods development for fast Magic-Angle Spinning (MAS) of the sample (on the order of 100 000 rotations per second) in the magnetic field.
Our group focuses on various aspects of NMR spectroscopy, both in terms of methods development as well as application to gain understanding of biology-related questions, and has been able to significantly drive the available methodology and as such the power of NMR in general forward. As such, we strive for methods enabling structure elucidation of proteins with increasing molecular size or which are characterized by significant sample heterogeneity, complex intermolecular interactions, or limitations in isotope-labeled protein expression. This concerns the structure of such proteins as well as the dynamics relevant for protein functionality. We develop new spectroscopic approaches as building blocks of our spectroscopic pulse schemes in conjunction with dedicated data processing schemes. Based on the developed methodology, we are in the position to give answers to questions about the details of specific proteins’ structure and dynamics, protein-water interactions, protein-ligand interactions, ligand mobility, and chemical mechanisms comprised in the active site.
See our (overview) Accounts paper on "Protons in Solid-State NMR"!
Our research is multi-faceted. The following sections try to describe excerpts of our striving in clusters similar character.
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Location & approach
The campus of TU Dortmund University is located close to interstate junction Dortmund West, where the Sauerlandlinie A 45 (Frankfurt-Dortmund) crosses the Ruhrschnellweg B 1 / A 40. The best interstate exit to take from A 45 is "Dortmund-Eichlinghofen" (closer to Campus Süd), and from B 1 / A 40 "Dortmund-Dorstfeld" (closer to Campus Nord). Signs for the university are located at both exits. Also, there is a new exit before you pass over the B 1-bridge leading into Dortmund.
To get from Campus Nord to Campus Süd by car, there is the connection via Vogelpothsweg/Baroper Straße. We recommend you leave your car on one of the parking lots at Campus Nord and use the H-Bahn (suspended monorail system), which conveniently connects the two campuses.
TU Dortmund University has its own train station ("Dortmund Universität"). From there, suburban trains (S-Bahn) leave for Dortmund main station ("Dortmund Hauptbahnhof") and Düsseldorf main station via the "Düsseldorf Airport Train Station" (take S-Bahn number 1, which leaves every 20 or 30 minutes). The university is easily reached from Bochum, Essen, Mülheim an der Ruhr and Duisburg.
You can also take the bus or subway train from Dortmund city to the university: From Dortmund main station, you can take any train bound for the Station "Stadtgarten", usually lines U41, U45, U 47 and U49. At "Stadtgarten" you switch trains and get on line U42 towards "Hombruch". Look out for the Station "An der Palmweide". From the bus stop just across the road, busses bound for TU Dortmund University leave every ten minutes (445, 447 and 462). Another option is to take the subway routes U41, U45, U47 and U49 from Dortmund main station to the stop "Dortmund Kampstraße". From there, take U43 or U44 to the stop "Dortmund Wittener Straße". Switch to bus line 447 and get off at "Dortmund Universität S".
The H-Bahn is one of the hallmarks of TU Dortmund University. There are two stations on Campus Nord. One ("Dortmund Universität S") is directly located at the suburban train stop, which connects the university directly with the city of Dortmund and the rest of the Ruhr Area. Also from this station, there are connections to the "Technologiepark" and (via Campus Süd) Eichlinghofen. The other station is located at the dining hall at Campus Nord and offers a direct connection to Campus Süd every five minutes.
The AirportExpress is a fast and convenient means of transport from Dortmund Airport (DTM) to Dortmund Central Station, taking you there in little more than 20 minutes. From Dortmund Central Station, you can continue to the university campus by interurban railway (S-Bahn). A larger range of international flight connections is offered at Düsseldorf Airport (DUS), which is about 60 kilometres away and can be directly reached by S-Bahn from the university station.
The facilities of TU Dortmund University are spread over two campuses, the larger Campus North and the smaller Campus South. Additionally, some areas of the university are located in the adjacent "Technologiepark".