Analysis of mutations predicted to destabilize the A2 domain.

<p>(<b>A</b>) C root mean square fluctuations of mutants compared to the wild-type. The values reported are averages over three runs. The bars indicate the standard error of the mean and the labels are the correlation p-values from a single-tailed student t-test (mutant versus wild-type). Reported are only p-values which are not larger than 0.1. (<b>B</b>) Van der Waals interaction energy between a side chain and the rest of the simulated system (i.e., rest of the protein and solvent). Compared are the energy of the wild-type residue (black) and the mutated side chain (red). The values are averages over three runs using the last 30 ns of in total 40 ns long runs at 300 K under static conditions (i.e., no force was applied). Electrostatic interaction energies are not shown because they are negligible compared to vdW. (<b>C</b>) Tensile force during exposure of the C-terminal hydrophobic core (see “Materials and Methods” for details about its measurement) in constant velocity pulling simulations with the mutants compared to the wild-type. The values are averaged over three runs and the standard error of the mean is indicated by error bars. The correlation p-values from the single tailed student t-test (mutant versus wild-type) are reported.