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. 2015 Dec 16;6:10172. doi: 10.1038/ncomms10172

Figure 7. NMR spectroscopy analysis of Hb binding to KdHpuA.

Figure 7

HSQC spectra were collected of 130 μM wild type, T124D and Δloop-1 KdHpuA alone, and with 13, 26, 39 and 65 μM Hb or BSA. (ad) HSQC spectra of the start (0 μM Hb/BSA—red) and end (65 μM Hb/BSA—black) points of titration of Hb into wild type (a), Hb into T124D (b), Hb into Δloop-1 (c) and BSA into wild type (d). (e) Chart showing the relative intensities of KdHpuA amide peaks as they decrease during titration with Hb but not with BSA.