Thomas R. Weikl 1, 2, Matteo Palassini 1, 3, Ken A. Dill 1
Protein Science 13 (2004) 822-829
We present a solvable model that predicts the folding kinetics of two-state proteins from their native structures. The model is based on conditional chain entropies. It assumes that folding processes are dominated by small-loop closure events that can be inferred from native structures. For CI2, the src SH3 domain, TNfn3, and protein L, the model reproduces two-state kinetics, and it predicts well the average Phi-values for secondary structures. The barrier to folding is the formation of predominantly local structures such as helices and hairpins, which are needed to bring nonlocal pairs of amino acids into contact.
- 1. Department of Pharmaceutical Chemistry,
University of California, San Francisco - 2. Max-Planck-institut für Kolloid – und Grenzflächenforschung,
Max-Planck-Institut - 3. Laboratoire de Physique Théorique et Modèles Statistiques (LPTMS),
CNRS : UMR8626 – Université Paris XI – Paris Sud