Figure 6 | Scientific Reports

Figure 6

From: ALS-causing mutations in profilin-1 alter its conformational dynamics: A computational approach to explain propensity for aggregation

Figure 6

The hairpin switch mechanism of isolated PFN1WT. (A–C) The GLU47-LYS70 salt bridge donor–acceptor distances for isolated (A) PFN1WT, (B) PFN1T109M, and (C) PFN1G118V during the 200-ns molecular dynamics simulations. (D–F) The distances between the Cα atom of G67 (tip of a hairpin) and the mass center of β-sheet for (A), PFN1T109M (B), and PFN1G118V (C). (G,H) Illustration of the GLU47-LYS70 salt bridge and twisting away of the G67 hairpin from the β-sheet (the hairpin switch mechanism) in the third Isolated PFN1WT simulations by showing the initial (G) and final (H) conformations of PFN1 in cartoon representation.

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