NMR studies of protein - DNA interactions

An overview of the nuclear magnetic resonance (NMR) techniques commonly used to get information on protein-DNA interactions is studied. It includes a brief description of DNA labeling techniques, the use of chemical shift or hydrogen exchange changes to find the binding site, the use of hydrogen exchange or relaxation data to get dynamics information on the binding process, the use of the main isotope filtering and editing techniques as well as transverse relaxation-optimized spectroscopy to assign the NMR signals and newly developed techniques to deal with large complexes or to obtain long range distance restraints. The second part comprises applications of these techniques to different protein-DNA complexes.