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. Author manuscript; available in PMC: 2020 Oct 31.
Published in final edited form as: J Phys Chem B. 2016 Feb 1;120(5):926–935. doi: 10.1021/acs.jpcb.5b11767

Figure 2:

Figure 2:

Implied timescale spectra of 40-macrostate MSMs for all eight protein sequences. Shown are the ten slowest timescales with error bars denoting uncertainties estimated from ten-fold cross-validation. Dashed lines are to guide the eye. For all sequences, the slowest timescale is well-separated from the rest, indicative of two-state helix folding. Sequences containing R14 (Fs-ERE, ERR, RRE and RRR) have slower folding times than those containing E14, with the greatest difference seen for Fs-EEE (~180 ns) versus Fs-ERE (~400 ns). On the right (gray panel) is shown a comparison of implied timescales for 1200-microstate and 40-macrostate MSMs built from the combined sequence data. Only a slight acceleration in timescales is seen in the macrostate model, indicating very modest artifacts due to coarse-graining.