TROSY-based NMR experiments for NMR studies of large biomolecules

摘要

Nuclear magnetic resonance (NMR) spectroscopy is the most powerful spectroscopic tool for structure–function studies of biological macromolecules in solution. Conventional multidimensional NMR spectroscopic methods developed before 1997 were limited to the study of proteins smaller than 25 and 60 kDa for ~(13)C/~(15)N and ~2H/~(13)C/~(15)Nlabeled proteins, respectively [1–3]. The introduction of Transverse Relaxation Optimized Spectroscopy (TROSY)-based NMR methods [4–9] opened new avenues for the structural determination of much larger biological macromolecules, particularly proteins and nucleic acids.