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A new assignment technique of 2D‐NMR spectra by spin‐lock sequence to a tripeptide containing tryptophan in water
Author(s) -
Watanabe Eiji,
Yamakura Fumiyuki,
Kan Hirosaki
Publication year - 2010
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.2567
Subject(s) - chemistry , pulsed field gradient , tryptophan , tripeptide , indole test , spectral line , field (mathematics) , spectrum (functional analysis) , analytical chemistry (journal) , stereochemistry , molecule , amino acid , chromatography , organic chemistry , physics , mathematics , quantum mechanics , pure mathematics , biochemistry , astronomy
Abstract We developed a new assignment technique of tryptophan residues using pulsed field gradient TOCSY–ROESY (PFG‐TORO) and pulsed field gradient TOCSY–ROESY–TOCSY (PFG‐TOROTO) techniques in water. Connectivity from βH to ζ2H (H‐7) via ε1H (H‐1) and δ1H (H‐2) in the TORO spectrum and from βH to ζ3H (H‐5) and η2H (H‐6) via ε1H (H‐1) and δ1H (H‐2) in the TOROTO spectrum could be able to assign each of the protons of the indole rings. Copyright © 2010 John Wiley & Sons, Ltd.