Figure 3 | Scientific Reports

Figure 3

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

Figure 3

Correlation between multi-point HR-HRPF data by comparing reactivities in denatured form (SlopeD) versus native form (SlopeN) and fractional <SASA> between native (<SASA>N) and denatured (<SASA>D) based on all non-sulfur containing residues from myoglobin (circles) and lysozyme (squares). Each data point represents an oxidized amino acid identified in both denatured and native sample. Red – highly reactive residues; Blue – moderately reactive residues; and Green – poorly reactive residues. 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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