Abstract
AbstractSequential assignment of amide resonances in proteins and peptides can conveniently be derived from two‐dimensional inter‐residue 15Ni–1HN(i−1) and intra‐residue 15Ni–1HNi correlation spectra. The inter‐residue 15Ni–1HN(i−1) correlation spectrum is generated by recording the 15Ni frequency evolution indirectly and subsequently transferring the magnetization to 1HN(i−1) of the preceding residue for direct detection. The flow of coherence is established by the (H)N(COCAHA)‐TOCSY pulse sequence. Following the path from intra‐residue correlation via inter‐residue correlation to the next intra‐residue correlation results in sequential assignment in two dimensions. This kind of assignment protocol is most amenable to re‐establishing sequential assignments of target proteins perturbed by binding of ligands or alternatively signals of peptide ligands can be traced in studies of structure–function relationships by NMR. Copyright © 2001 John Wiley & Sons, Ltd.
Published Version
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