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The Effect of Tensile Stress on the Conformational Free Energy Landscape of Disulfide Bonds

Figure 4

Stress–strain relation of disulfide bonds parameterized by the response of the C_α–C_α distance to tensile force.

Dependence of the computed average distance between the C_α–atoms as a function of for the polypeptide model (black circles), cystine (red circles), and DEDS (green circles) depicted in Fig. 1 and obtained from force field equilibrium (at zero force) and force clamp MD (for nN) simulations. Computational reference data for DEDS obtained from QM/MM simulations are shown by brown triangles and the experimental reference based on the strained macrocycle [27] (see text) is marked by a violet square. The horizontal blue, pink and orange dotted lines are the average C_α–C_α distances of disulfide bonds in TDi, DO and interchain Ig proteins, respectively, whereas the cyan dotted line corresponds to intrachain Ig proteins; these averages have been computed using the identical data sets as those that underly Fig. 3, see caption.

doi: https://doi.org/10.1371/journal.pone.0108812.g004