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Significance In spite of recent advances made in computer simulation techniques, one of the main challenges in the protein-folding field is to bridge microscopic motions and experimental measurements. This paper demonstrates that the physics-based, coarse-grained united-residue (UNRES) force field, which has the ability to simulate folding of small- and midsize proteins in the millisecond timescale, can predict the folding kinetics correctly and bridge theoretical and experimental worlds. The results suggest that the use of the UNRES force field will open a new door to the understanding of protein motions at much longer timescales and help explain the differences between theoretical results and experimental observations.

Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements