Thermodynamics of the Trp-cage miniprotein unfolding in urea.

Proteins
Lucas N R WaferG I Makhatadze

Abstract

The thermodynamic properties of unfolding of the Trp-cage mini protein in the presence of various concentrations of urea have been characterized using temperature-induced unfolding monitored by far-UV circular dichroism spectroscopy. Analysis of the data using a two-state model allowed the calculation of the Gibbs energy of unfolding at 25 degrees C as a function of urea concentration. This in turn was analyzed by the linear extrapolation model that yielded the dependence of Gibbs energy on urea concentration, i.e. the m-value for Trp-cage unfolding. The m-value obtained from the experimental data, as well as the experimental heat capacity change upon unfolding, were correlated with the structural parameters derived from the three dimensional structure of Trp-cage. It is shown that the m-value can be predicted well using a transfer model, while the heat capacity changes are in very good agreement with the empirical models based on model compounds studies. These results provide direct evidence that Trp-cage, despite its small size, is an excellent model for studies of protein unfolding and provide thermodynamic data that can be used to compare with atomistic computer simulations.

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Citations

Jan 13, 2011·Biochemistry·D Victoria WilliamsNiels H Andersen
Oct 8, 2011·Journal of the American Chemical Society·Agustina Rodriguez-GranilloVikas Nanda
Oct 26, 2012·Journal of the American Chemical Society·Bryan F ShawGeorge M Whitesides
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Jan 15, 2020·The Journal of Physical Chemistry Letters·Farzaneh ChalyaviMatthew J Tucker
Nov 14, 2019·The Journal of Physical Chemistry Letters·Pritam Ganguly, Joan-Emma Shea

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