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. 2017 Dec 7;12(12):e0189064. doi: 10.1371/journal.pone.0189064

Fig 3. Molecular dynamics (MD) were used to simulate the affect of mutating protiens to CS and ΔCS.

Fig 3

Critical residues for each of the structure are red and were calculated independently. A) 52% of noncritical human myoglobin residues were changed. The CS structure is superimposed on top of the WT human myoglobin structure. B) The critical residues of human myoglobin were changed to alanine residues, accounting for 12% of the residues in the structure. The ΔCS protein is superimposed on top of the WT human myoglobin structure. C) The RMSD for CS and ΔCS myoglobin is plotted for the MD simulation. D) The CS p53 with 53% of WT residues changed superimposed on the WT protein. E) The ΔCS p53 with 15% of residues changed superimposed on the WT protein. F) The RMSD for CS and ΔCS p53 is plotted for the MD simulation. G) The CS sushi domain 15 of complement factor H with 47% of WT residues changed superimposed on the WT protein. H) The ΔCS sushi domain 15 of complement factor H with 23% of residues changed superimposed on the WT protein. I) The RMSD for CS and ΔCS sushi domain 15 of complement factor H is plotted for the MD simulation.