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Structural Basis of Type 2A von Willebrand Disease Investigated by Molecular Dynamics Simulations and Experiments

Figure 4

Time series of quantities measured during the pulling simulation WT_pull_1.

Qualitatively similar unfolding pathways were observed in all runs with the wild-type and mutants (see Figures S4, S5, S6, S7, S8, S9, S10, S11, S12, S13, S14). (A) Applied tensile force. Events observed during the simulations corresponding to force peaks (i.e., sharp increases followed by drops) are indicated. (B) Formation of secondary structure elements. The colors are explained in the legend on the right. The position of the Tyr-Met cleavage site is indicated by a red line and labeled on the right. (C) C RMSD of the two C-terminus proximal helices 5 and 6. (D) Solvent accessible surface area of the Tyr-Met cleavage site. (E) C RMSD from the native state for the N-terminal part of the (residues 1497 to 1605) and the C-terminal part of the protein (residues 1606 to 1668). (F) Solvent accessible surface area of the minimum docking unit for ADAMTS13 (residues 1645–1668) identified in a previous experimental study [28].

Figure 4

doi: https://doi.org/10.1371/journal.pone.0045207.g004