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. Author manuscript; available in PMC: 2023 Aug 1.
Published in final edited form as: Biophys Chem. 2022 Apr 29;287:106821. doi: 10.1016/j.bpc.2022.106821

Figure 3. Effect of size and folding mechanism on protein folding rates.

Figure 3.

(A) Plot illustrating the dependence of protein folding rate constant (kf) on the number of residues for two-state folding proteins. Small (<50 residues) two-state proteins fold quickly with ln(kf) > 9.4 (green box). Many larger two-state folders fold more slowly (orange box). (B) Dependence of protein folding rate constant (kf) on the number of residues for multi-state folding proteins. Large (>200 residues) multi-state proteins have the slowest folding rates, with ln(kf) <−2.5 (red box). A list of the proteins and references for the data in this plot is available as Supplementary Information Table S1.