Abstract
Assignment procedures for backbone resonances of proteins are outlined for homonuclear and heteronuclear three-dimensional NMR spectroscopy. Phasecycling procedures in fast 3D experiments are discussed. Examples of data space reducing processing techniques are given. A new triple resonance based assignment procedure for protein resonances is outlined. The general advantages and disadvantages of homonuclear and heteronuclear three-dimensional NMR spectroscopy are discussed.
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