PathMolD-AB: Spatiotemporal pathways of protein folding using parallel molecular dynamics with a coarse-grained model.

Solving the protein folding problem (PFP) is one of the grand challenges still open in computational biophysics. Globular proteins are believed to evolve from initial configurations through folding pathways connecting several thermodynamically accessible states in a free energy landscape until reaching its minimum, inhabited by the stable native structures. Despite its huge computational burden, molecular dynamics (MD) is the leading approach in the PFP studies by preserving the Newtonian temporal evolution in the canonical ensemble.

A benchmark of optimally folded protein structures using integer programming and the 3D-HP-SC model.

The Protein Structure Prediction (PSP) problem comprises, among other issues, forecasting the three-dimensional native structure of proteins using only their primary structure information. Most computational studies in this area use synthetic data instead of real biological data. However, the closer to the real-world, the more the impact of results and their applicability.