Abstract
The two-dimensional J -resolved H NMR spectra at 360 MHz of the 20 common amino acids have been investigated. The characteristic features of strong coupling are described. Advantages and drawbacks of projections, cross sections, and contour plots for the presentation of spectra including strong coupling are illustrated with selected examples. On the basis of the amino acid data practical aspects of the use of two-dimensional J -resolved spectroscopy to improve the resolution of high-field 1 H NMR spectra of proteins are discussed.
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