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. 2009;48(31):5708-10.
doi: 10.1002/anie.200901520.

Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy

Marvin J Bayro  1 , Thorsten Maly, Neil R Birkett, Christopher M Dobson, Robert G Griffin
Affiliations

Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy

Marvin J Bayro et al. Angew Chem Int Ed Engl. 2009.
No abstract available

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Figures

Figure 1
Figure 1
(a) Band selective RFDR pulse sequence for two-dimensional homonuclear correlation spectroscopy. The recoupling π pulses occupy half or more of the rotor period, τr, and follow a 32-step phase scheme. (b) Long-range aliphatic correlation spectrum of 2-PI3-SH3 amyloid fibrils obtained with 17.92 ms of longitudinal mixing via BASE RFDR. The mixing time was optimized for 3.8 Å, typical internuclear distance of sequential Cα-Cα contacts. The spectrum was recorded in 27 hrs at 16.4 T magnetic field and 12.5 kHz MAS frequency, with 12.5 kHz 13C recoupling π pulses centered at 48 ppm.
Figure 2
Figure 2
Long-range aliphatic correlations in 2-PI3-SH3 obtained with 17.92 ms of BASE RFDR (a) and 500 ms of DARR (b). Both spectra were recorded in 6.8 hrs under similar experimental conditions to those described for Fig. 1(b). BASE RFDR shows improved overall polarization transfer efficiency, highlighted by dashed ellipses. Dotted ellipses mark a few exceptions, likely the result of remaining dipolar truncation for certain spin systems. See the supporting information for full spectral views.
See this image and copyright information in PMC

References

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