[en] The determination of protein structure by NMR is restricted at molecular masses above 10 k Da by overlapping resonances. One way of overcoming this problem is to label the protein with 15N. The conventional way to record 15N spectra is to use heteronuclear multiple-quantum coherence. We present here an alternative approach based on 15N single-quantum coherence. This is shown to have substantial advantages over the multiple-quantum method, including better F1 resolution. (author). 23 refs.; 2 figs
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