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Sequential resonance assignment from two‐dimensional inter‐ and intra‐residue 15 N– 1 H correlation spectra
Author(s) -
Perttu Permi,
Arto Annila
Publication year - 2001
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.821
Subject(s) - chemistry , residue (chemistry) , pulse sequence , amide , spectral line , correlation , two dimensional nuclear magnetic resonance spectroscopy , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , stereochemistry , analytical chemistry (journal) , crystallography , physics , chromatography , geometry , mathematics , organic chemistry , quantum mechanics
Sequential assignment of amide resonances in proteins and peptides can conveniently be derived from two‐dimensional inter‐residue 15 N i – 1 H N ( i −1) and intra‐residue 15 N i – 1 H N i correlation spectra. The inter‐residue 15 N i – 1 H N ( i −1) correlation spectrum is generated by recording the 15 N i frequency evolution indirectly and subsequently transferring the magnetization to 1 H N ( 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.