Robert Powers (National Institutes of Health, Bethesda, Md.): “Recent advances in NMR and simulated annealing techniques have made it possible to solve structures of proteins in solution at a resolution comparable to a 2 Å crystal structure. The availability of 13C/15N-labeled proteins and the application of multidimensional heteronuclear NMR pulse sequences have enabled proteins of increasing size (20 KDa) and biological interest to be analyzed by NMR. These developments have increased the popularity and practicality of NMR as an approach to studying the structure and function of proteins, which in turn accounts for the large number of citations this paper has received since its publication.
“An inherent drawback of multidimensional NMR is the additional time required to acquire a spectrum. To keep measuring times within reasonable limits (1.5 to 3 days), spectra are usually recorded with coarse digitization, which results in a loss of resolution.