# Protein folding rates correlate with heterogeneity of folding mechanism

Source: [Protein folding rates correlate with heterogeneity of folding mechanism](<https://www.sota2.com/research/paper/68fa5e951e209131ce9e38ea>)

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

Data updated: 2025-10-25T18:52:48.052Z

Authors: B. \\"Oztop, M. R. Ejtehadi, S. S. Plotkin

Published: 2004-07-14T22:33:59.000Z

## Abstract

By observing trends in the folding kinetics of experimental 2-state proteins at their transition midpoints, and by observing trends in the barrier heights of numerous simulations of coarse grained, C-alpha model, Go proteins, we show that folding rates correlate with the degree of heterogeneity in the formation of native contacts. Statistically significant correlations are observed between folding rates and measures of heterogeneity inherent in the native topology, as well as between rates and the variance in the distribution of either experimentally measured or simulated phi-values.

## 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/0407022>)

[PDF](<https://arxiv.org/pdf/q-bio/0407022.pdf>)
