Thermodynamic characterization of URN1-FF at different pHs.

1<p>Gibbs energy of unfolding with urea determined from the equilibrium parameters.</p>2<p>Dependence of the Gibbs energy of unfolding with urea.</p>3<p>The urea concentration required to unfold 50% of the protein molecules.</p>4<p>Parameters obtained by following changes in the molar ellipticity at 222 nm.</p>5<p>Parameters obtained by following changes in the intrinsic fluorescence at 350 nm.</p>6<p>The values of the FF domain of HYPA/FBP11 were previously reported at 283 K <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0058297#pone.0058297-Jemth1" target="_blank">[18]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0058297#pone.0058297-Jemth2" target="_blank">[19]</a>.