A new assignment technique of 2D-NMR spectra by spin-lock sequence to a tripeptide containing tryptophan in water.
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 betaH to zeta2H (H-7) via epsilon1H (H-1) and delta1H (H-2) in the TORO spectrum and from betaH to zeta3H (H-5) and eta2H (H-6) via epsilon1H (H-1) and delta1H (H-2) in the TOROTO spectrum could be able to assign each of the protons of the indole rings.
Watanabe
Eiji
E
Department of Chemistry, Rikkyo University, Toshima-ku, Tokyo 171-8501, Japan. eiji-jun@umin.ac.jp
Yamakura
Fumiyuki
F
Kan
Hirosaki
H
D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009842:Oligopeptides / Q000737:chemistry*; D012015:Reference Standards; D014364:Tryptophan / Q000032:analysis* / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D009842:Oligopeptides; D014867:Water; C029535:lysyl-tryptophyl-alpha-lysine; D014364:Tryptophan