Probing the potential of ureasil-poly(ethylene oxide) as a glyphosate scavenger in aqueous milieu: force-field parameterization and MD simulations

The intensive use of glyphosate in conventional agriculture and its high solubility in water have led to contamination of aqueous systems worldwide.

Development of accurate coarse-grained force fields for weakly polar groups by an indirect parameterization strategy

An indirect coarse-grained force field parameterization strategy for weakly polar groups.

Molecular simulation of osmometry in aqueous solutions of the BMIMCl ionic liquid: a potential route to force field parameterization of liquid mixtures

By means of molecular simulation, the osmotic coefficient of aqueous solution of BMIMCl ionic liquid is calculated to compare with the experimental data and use that to optimize two popular force fields available in the literature for bulk ILs.

Exploiting a Mechanical Perturbation of Titin Domain to Identify How Force Field Parameterization Affects Protein Refolding Pathways

Molecular mechanics force fields have been shown to differ in their predictions of processes such as protein folding. To test how force field differences affect predicted protein behavior, we created a mechanically perturbed model of the beta-stranded I91 titin domain based on atomic force spectroscopy data and examined its refolding behavior using six different force fields. To examine the transferability of the force field discrepancies identified by this model, we compared the results to equilibrium simulations of the weakly helical peptide Ac-(AAQAA)3-NH2. The total simulation time was 80 µs. From these simulations we found significant differences in I91 perturbation refolding ability between force fields. Concurrently, Ac-(AAQAA)3-NH2 equilibration experiments indicated that although force fields have similar overall helical frequencies, they can differ in helical lifetimes. The combination of these results suggests that differences in force field parameterization may allow a more direct transition between the beta and alpha regions of the Ramachandran plot thereby affecting both beta-strand refolding ability and helical lifetimes. Furthermore, the combination of results suggests that using mechanically perturbed models can provide a controlled method to gain more insight into how force fields affect protein behavior.