Recent progress has permitted observation of reproducible folding of small proteins in molecular dynamics simulations(1, 2). Despite the availability of transferable forcefields, these methods remain constrained by the short time-step and availability of specialized hardware. using a new Monte-Carlo based biomolecular simulation code, SIMONA(3), with a modified AMBER forcefield we observe rapid reproducible folding transitions in single-PC simulations of several small proteins, including the villin headpiece and the WW-domain, which can be used to completely characterize the protein folding equilibrium at the all-atom level. These results demonstrate that Monte-Carlo methods can significantly accelerate sampling of large-scale conformational changes of proteins on widely accessible computational resources.1. Lindorff-Larsen, K., et. al. Science 334, 517-520. (2012)2. Shaw, D. E., et.al. Science 330, 341-346 (2010).3. Strunk, T., et. al. SIMONA 1.0: An efficient and versatile framework for stochastic simulations of molecular and nanoscale systems, J. Comp. Chem, DOI: 10.1002/jcc.23089. (2012)View Large Image | View Hi-Res Image | Download PowerPoint Slide