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. 2005 Mar 15;102(13):4765–4770. doi: 10.1073/pnas.0409538102

Fig. 5.

Fig. 5.

Comparison of amide proton protection in the equilibrium intermediate at pH 4 and in the burst-phase intermediate, plotted onto the fully folded structure of myoglobin. (a) Amide proton protection measured in DMSO, using the interrupted H/D-exchange method. Red spheres show amides with high protection (protection factor of >10 in Fig. 2), green spheres indicate amides with medium protection (7 < protection factor < 10), and blue spheres show amides with low protection (protection factor of <7). (b) Amide proton protection in the burst-phase kinetic intermediate, measured in DMSO after the quench-flow pH-pulse-labeling experiment. Red spheres show high protection (proton occupancy >0.7 in Fig. 4), green spheres show medium protection (0.4 < proton occupancy <0.7), and blue spheres indicate low occupancy (proton occupancy <0.4).