Figure 2 | Scientific Reports

Figure 2

From: Quantitative Protein Topography Measurements by High Resolution Hydroxyl Radical Protein Footprinting Enable Accurate Molecular Model Selection

Figure 2

Correlation plots of NPF (the slope of the linear regression divided by the inherent reactivity of the free amino acid) vs. fractional <SASA> (<SASA> of the amino acid in the folded structure divided by the <SASA> for that same amino acid in a Gly-X-Gly tripeptide) for amino acids identified to be oxidized from lysozyme (green square) and myoglobin (red circle) sample for: (a) amino acids with high inherent reactivity (>10x more reactive than Pro); (b) amino acids with moderate inherent reactivity (4–10x more reactive than Pro); (c) amino acids with poor inherent reactivity (<4x more reactive than Pro). All data shown from triplicate experiments using mean ± SD plotted for all data (x-axis error bars), with fractional <SASA> from MD simulation of the protein structure ± SD from the MD trajectory (y-axis error bars).

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