Extended Data Fig. 2: The anti-TROSY component of 19F-attached 13C relaxes out of the equation. | Nature Chemistry

Extended Data Fig. 2: The anti-TROSY component of 19F-attached 13C relaxes out of the equation.

From: Leveraging relaxation-optimized 1H–13CF correlations in 4-19F-phenylalanine as atomic beacons for probing structure and dynamics of large proteins

Extended Data Fig. 2

(a–c) T2-modulated 1H-13C HSQC spectra of hCAII (29 kDa) at 25°C. The relaxation delays during 13C evolution were set to (a) 0 ms, (b) 8 ms and (c) 12 ms. Dashed red lines connect TROSY and anti-TROSY components along the 13C dimension. A few example peak-pairs were chosen for illustration. (d) Overlay of two HCF-TROSY spectra of hCAII (29 kDa) at 25 °C are shown. One spectrum was recorded with 19F-13C TROSY selection at 600 MHz (blue). The second spectrum was recorded without fluorine selection on a spectrometer not equipped with a fluorine NMR capable probe at 800 MHz (green). The empty space to the left of the spectrum is the space where one would expect anti-TROSY peaks if they were present in the spectrum.

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