# Concentration-Temperature Superposition of Helix Folding Rates in Gelatin

Source: [Concentration-Temperature Superposition of Helix Folding Rates in Gelatin](<https://www.sota2.com/research/paper/68fa27462c2a3760193c19ad>)

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

Data updated: 2025-10-24T11:54:49.736Z

Authors: J.L. Gornall, E.M. Terentjev

Published: 2006-02-07T19:06:15.000Z

## Abstract

We study the kinetics of helix-coil transition in water solutions of gelatin (collagen protein) by optical rotation techniques combined with thermal characterization. By examining the rates of secondary helix folding, and covering a very wide range of solution concentrations, we are able to identify a universal exponential dependence of folding rate on concentration and quench temperature. We demonstrate a new concentration-temperature superposition of data at all temperatures and concentrations, and build the corresponding master curve. The results support the concept of a diffuse helix-coil transition. We find no concentration dependance of the normalized rate constant, suggesting first order (single) kinetics of secondary helix folding dominate in the early stages of renaturation.

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## Original sources and implementation

[Original paper](<https://arxiv.org/abs/cond-mat/0602188>)

[PDF](<https://arxiv.org/pdf/cond-mat/0602188.pdf>)