# Cooperativity in two-state protein folding kinetics

Source: [Cooperativity in two-state protein folding kinetics](<https://www.sota2.com/research/paper/68fa1fd37a2b558e2932c833>)

Collection index: [llms.txt](<https://www.sota2.com/research/llms.txt>)

Data updated: 2025-10-23T19:45:42.542Z

Authors: Thomas R. Weikl, Matteo Palassini, Ken A. Dill

Published: 2003-11-06T16:45:19.000Z

## Abstract

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.

## Recorded benchmark results

A research result applies to its stated dataset, split, metric and evaluation configuration. Compare like-for-like settings, preserve the metric's unit and direction, and distinguish paper-reported results from independent reproduction. The best result recorded here is not a claim of exhaustive, current global coverage.

## Original sources and implementation

[Original paper](<https://arxiv.org/abs/q-bio/0311004>)

[PDF](<https://arxiv.org/pdf/q-bio/0311004.pdf>)