TOCSYTotal Correlation Spectroscopy (NMR technique)
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TOCSY cross peaks at 2.483, 3.535, and 3.703 ppm are in accordance with the 3-HIB HMDB entry 00023 values of 2.4727, 3.5244, and 3.6844.
1H-NMR, 13C-NMR, HMBC, HMQC, COSY, and TOCSY spect-ra were recorded in deuterated solvents on Bruker-AVANCE spectrometers on 100, 300, 400, 500, and 600 MHz.
The assignments of the peptide resonances were made by a combination of mono- and bidimensional and multinuclear NMR techniques [sup.1]H-[sup.1]H TOCSY, [sup.1]H-[sup.13]C HSQC, and [sup.1]H-[sup.1]H ROESY at different pH values.
[sup.1]H-NMR and TOCSY, COSY, HMBC, HMQC, and NOESY spectra were recorded at 21[degrees]C on a Varian Unity Inova 600 NMR spectrometer using Varian VNMRJ software.
Figure 6B illustrates the shift effect of the cross-peaks of the side chain mannose units by the addition of an [alpha]-or [beta]-mannose unit observed in the TOCSY spectrum of Fig.
The pulse delay for TOCSY experiment the mixing time was set at 80 ms.
Characterization of the fraction components using 1D TOCSY and 1D ROESY experiments.
This second edition contains new material on the new 2D NMR techniques TOCSY, HMQC, and HMBC, and new treatment of the Fourier transform ion cyclotron resonance MS.
The reader learns of the growing application of NMR (nuclear magnetic resonance) to the study of protein structure, with its 3 pulse schemes, COSY (correlation spectroscopy), TOCSY (total correlation spectroscopy), and NOESY (nuclear Overhauser effect spectroscopy).
The peaks were assigned in the proton spectra using 2D NMR methods (COSY and TOCSY) and in the carbon spectrum using DEPT.
Newly developed 2D NMR techniques include totally correlated spectroscopy (TOCSY) and maximum quantum spectroscopy (MAXY).
The two dimensional experiments include the TOCSY and the NOESY and distances are obtained from the nuclear Overhauser effect.