Chain length is the main determinant of the folding rate for proteins with three‐state folding kinetics

@article{Galzitskaya2003ChainLI,
  title={Chain length is the main determinant of the folding rate for proteins with three‐state folding kinetics},
  author={Oxana V. Galzitskaya and Sergiy O. Garbuzynskiy and Dmitry N. Ivankov and Alexei V. Finkelstein},
  journal={Proteins: Structure},
  year={2003},
  volume={51}
}
We demonstrate that chain length is the main determinant of the folding rate for proteins with the three‐state folding kinetics. The logarithm of their folding rate in water (kf) strongly anticorrelates with their chain length L (the correlation coefficient being −0.80). At the same time, the chain length has no correlation with the folding rate for two‐state folding proteins (the correlation coefficient is −0.07). Another significant difference of these two groups of proteins is a strong… 
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    2009 3rd International Conference on Bioinformatics and Biomedical Engineering
  • 2009
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TLDR
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General mechanism of two-state protein folding kinetics.
TLDR
This model predicts that the free energy landscape has a volcano shape, rather than a simple funnel, that folding is two-state (single-exponential) when secondary structures are intrinsically unstable, and that each structure along the folding path is a transition state for the previous structure.
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It is shown that the Abs_CO = CO × L, is able to predict rather accurately folding rates for both two‐state and multistate folding proteins, as well as short peptides, and that thisAbs_CO scales with the protein chain length as L0.70 ± 0.07 for the totality of studied single‐domain proteins and peptides.
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