Resonance assignment strategies for Small Proteins

Abstract Prior to 1982, assignment of resonances in the complex NMR spectra of proteins was achieved, using ID NMR, and was based, for the most part, on the assumption that the structure of the protein in solution was the same as in the available X-ray structure. The introduction of 2D NMR techniques such as COSY and NOESY in the early 1980s dramatically increased the resolution of protein NMR spectra and as a result the amount of information which could be obtained from these spectra also increased. In 1982 With rich and co-workers introduced a systematic method for the full assignment of the 2D NMR spectra of proteins which relied only on information about the amino acid sequence of the protein; this method is the sequential assignment procedure (1,2). This approach is now used by most researchers who apply NMR spectroscopy to the study of proteins.