This review discusses Gō models broadly used in biomolecular simulations. I start with a
brief description of the original lattice model study by Nobuhiro Gō. Then, the theory of …

Recent breakthroughs in highly accurate protein structure prediction using deep neural
networks have made considerable progress in solving the structure prediction component of …

Despite the recent advances in the prediction of protein structures by deep neutral networks,
the elucidation of protein-folding mechanisms remains challenging. A promising theory for …

Advances in computing have enabled microsecond all-atom molecular dynamics trajectories
of protein folding that can be used to compare with and test critical assumptions of …

We describe here a general model of the kinetic mechanism of protein folding. In the Foldon
Funnel Model, proteins fold in units of secondary structures, which form sequentially along …

Charged residues on the surface of a protein are known hot-spots for post-translational
modification, protein/ligand-binding, and tuning conformational stabilities. Recent …

The hydrophobic effect stabilizes the native structure of proteins by minimizing the
unfavorable interactions between hydrophobic residues and water through the formation of …

Statistical mechanical models that afford an intermediate resolution between macroscopic
chemical models and all-atom simulations have been successful in capturing folding …

Intrinsically disordered proteins (IDPs) and proteins with a large degree of disorder are
abundant in the proteomes of eukaryotes and viruses, and play a vital role in cellular …

Downhill folding proteins fold in microseconds by crossing a very low or no free energy
barrier (< 3 RT), and exhibit a complex unfolding behavior in equilibrium. Such unfolding …