<p>*For these proteins, <i>T</i>* values were not reported, but instead, the <i>T</i><sub>max</sub>, <i>E</i><sub>a</sub> and <i>v</i> values were given. The <i>T</i>* values were thus calculated by the relation: <i>T</i>* = (<i>RT</i><sub>max</sub><sup>2</sup>/<i>E</i><sub>a</sub>)×ln (<i>RT</i><sub>max</sub><sup>2</sup>/<i>E</i><sub>a</sub><i>v</i>) + <i>T</i><sub>max</sub>. <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0115877#pone.0115877-SanchezRuiz3" target="_blank">[5]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0115877#pone.0115877-ConejeroLara1" target="_blank">[66]</a>.</p>†<p>Determined by SDS polyacrylamide gel electrophoresis.</p>‡<p>Solubilized in 100 mM octy-β-D-glucopyra...
Information on changes in heat capacity (¿Cp) of proteins upon unfolding is used frequently in liter...
A theoretical analysis of several protein denaturation models (Lumry-Eyring models) that include a r...
The denaturation of proteins is an irreversible change of their coIIoidal properties by the followin...
The denatured states of proteins have always attracted our attention due to the fact that the denatu...
<p>A) Representative DSC traces obtained at 3°C/min; Lines are best-fits from a two-state irreversib...
To understand relationships between protein sequence and stability, we often compare data from prote...
<p><sup>a</sup> Values taken from [<a href="http://www.plosone.org/article/info:doi/10.1371/journal....
<p>The simulations shown are identical to that displayed in <a href="http://www.plosone.org/article/...
Differential scanning calorimetry has many advantages over other techniques to study the thermal sta...
<p>Heat induced unfolding curves of HPR and its variants are shown as plots of <i>f</i><sub>D</sub> ...
<p>(A) Protein theoretical isoelectric point (pI), and (B) hydrophobicity, between the heat-shock in...
<p>(A) and (B) Illustrative plots of activity versus time for experiments performed at several tempe...
Globular protein thermostability is characterized the cold denaturation, maximal stability $(T_{ms})...
<p>* The PDB IDs of Thermophilic (TS), Mesophilic (MS) pair, starting from Column 2, belong to famil...
AbstractGlobular protein thermostability is characterized the cold denaturation, maximal stability (...
Information on changes in heat capacity (¿Cp) of proteins upon unfolding is used frequently in liter...
A theoretical analysis of several protein denaturation models (Lumry-Eyring models) that include a r...
The denaturation of proteins is an irreversible change of their coIIoidal properties by the followin...
The denatured states of proteins have always attracted our attention due to the fact that the denatu...
<p>A) Representative DSC traces obtained at 3°C/min; Lines are best-fits from a two-state irreversib...
To understand relationships between protein sequence and stability, we often compare data from prote...
<p><sup>a</sup> Values taken from [<a href="http://www.plosone.org/article/info:doi/10.1371/journal....
<p>The simulations shown are identical to that displayed in <a href="http://www.plosone.org/article/...
Differential scanning calorimetry has many advantages over other techniques to study the thermal sta...
<p>Heat induced unfolding curves of HPR and its variants are shown as plots of <i>f</i><sub>D</sub> ...
<p>(A) Protein theoretical isoelectric point (pI), and (B) hydrophobicity, between the heat-shock in...
<p>(A) and (B) Illustrative plots of activity versus time for experiments performed at several tempe...
Globular protein thermostability is characterized the cold denaturation, maximal stability $(T_{ms})...
<p>* The PDB IDs of Thermophilic (TS), Mesophilic (MS) pair, starting from Column 2, belong to famil...
AbstractGlobular protein thermostability is characterized the cold denaturation, maximal stability (...
Information on changes in heat capacity (¿Cp) of proteins upon unfolding is used frequently in liter...
A theoretical analysis of several protein denaturation models (Lumry-Eyring models) that include a r...
The denaturation of proteins is an irreversible change of their coIIoidal properties by the followin...