Nuclear Magnetic Resonance (NMR) spectroscopy is the method of choice to detect and quantify biologically important motions in a near cellular environment. Using dedicated experiments we can probe motions ranging from the pico- to nanosecond time-scale up to the second time-scale, with atomic resolution. In addition, we can monitor how the molecular motions are affected by the interaction with adaptor complexes.
Traditionally, the application of NMR spectroscopy has been limited to complexes below 25 kDa in molecular weight. Recent advances have, however extended this molecular weight regime into the hundreds of kDa and in favorable cases over 1 MDa. This makes the large complexes involved in mRNA decay amenable to detailed studies of molecular dynamics. On the campus of the Max Planck Institute for Developmental Biology in Tübingen we now have 2 brand new NMR spectrometers installed (600 MHz and 800 MHz).
In summary, we hope to obtain a complete picture of protein dynamics and the modulation thereof. These aspects are fundamental to the understanding of the delicate balance between mRNA synthesis and degradation that allows the cell to regulate cellular processes by rapidly switching specific genes on or off.
Figure 3: 600 and 800 MHz NMR machines at the Tuebingen Campus, Germany