Concentration-Temperature Superposition of Helix Folding Rates in Gelatin

Details Concentration-Temperature Superposition of Helix Folding Rates in Gelatin Concentration-Temperature Superposition of Helix Folding Rates in Gelatin

2006-02-07

arxiv.org/abs/cond-mat/0602188v2

Physics

Condensed Matter

Soft Condensed Matter

6 figures

Scientific paper

10.1103/PhysRevLett.99.028304

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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