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. 2016 May 4;12(5):e1005585. doi: 10.1371/journal.ppat.1005585

Fig 7. Biophysical studies demonstrate MnaA and Cap5P bind tunicamycin.

Fig 7

(A, D) 600 MHz 1H NMR spectra of 15 μM tunicamycin. (B, E) 1H NMR STD spectra of 15 μM tunicamycin without 2-epimerase. (C) 1H NMR STD spectra of 15 μM tunicamycin in presence of 5 μM MnaA. (F) 1H NMR STD spectra of 15 μM tunicamycin in presence of 5 μM Cap5P. Saturation of the protein was achieved with a Gaussian pulse cascade resulting in a total saturation time of 3s. The protein resonances were saturated at 100 Hz and the off resonance was set to -120 ppm. Tunicamycin-specific peaks in NMR STD spectra were only obtained in the presence of MnaA or Cap5P. (G) Structure of tunicamycin.