Fig. 2: Efficiency of REHT in comparison to REST2 in capturing the folding of fast-folding protein, Trp-Cage. | Nature Communications

Fig. 2: Efficiency of REHT in comparison to REST2 in capturing the folding of fast-folding protein, Trp-Cage.

From: High resolution ensemble description of metamorphic and intrinsically disordered proteins using an efficient hybrid parallel tempering scheme

Fig. 2

a Structural overlay between the natively folded NMR structure (blue) and the REHT-generated folded structure of Trp-cage (yellow, obtained at the base replica). b Time evolution of protein backbone RMSD from the NMR structure along one of the successfully folded replicas of REHT (top) and REST2 (bottom) simulations. The RMSD evolution of other folded replicas are shown in Supplementary Figs. 4 and 5. c, d Free energy landscape of Trp-Cage, shown as the function of Radius of gyration (Rg) and RMSD against the NMR structure. The landscape is shown for the ensembles collected at the base replica of c) REHT simulation and d REST2 simulation.

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