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. Author manuscript; available in PMC: 2016 Jul 3.
Published in final edited form as: J Mol Biol. 2015 Apr 16;427(13):2319–2328. doi: 10.1016/j.jmb.2015.04.004

Fig. 2.

Fig. 2

(A) The aliphatic region of a 2D CHHC NMR spectrum of Sample A, showing a Cα-Cα cross-peak between M35 and G37 at 200 μs 1H spin diffusion period (colored circles). In the 2D CHHC spectrum, the solid colored lines indicate single-bond exchange pathways or residue-specific assignments for M35 (orange) and G37 (blue) determined from the 2D fpRFDR spectrum in Fig. 1. (B) A horizontal slice of the 2D CHHC spectrum taken at the position of the M35 Cα signal, indicated by the orange dashed line from Panel A (at 52.7ppm), is compared to a horizontal slice of the 2D fpRFDR spectrum in Fig. 1 taken at the position of the G37 Cα signal (43.8 ppm). The blue vertical dashed line with an arrow head indicates polarization transfer between the G37 and M35 Cα atoms.