<p>Experimental conditions were 50/acetate at pH 4.0 or glycine/HCl at the other pH values. Experimental data are represented by gray symbols whereas solid lines through are the best fitting obtained from respective DSC models as described in the text.</p
<p>The GdmCl concentration was taken for 50% of the protein fraction unfolded each and melting tempe...
<p>(A): Wild type (Black) and V42M (Brown) fitted curves were obtained from cursor initiative fittin...
<p>The thermal stability of wildtype SOD1 and SOD1<sup>G93A</sup> mutants was assessed at two concen...
<p>Protein concentration was 1.3·mL<sup>−1</sup> under 50 mM buffer, either acetic/acetate at pH 4.0...
<p>*Experimental conditions were 50 mM acetic/acetate pH 4.0; 50 mM Glycine/HCl pH 2.5–3.5. The erro...
<p>Thermal unfolding curves recorded from 25 to 90°C were expressed as fraction folded derived from ...
New approaches to the analysis of differential scanning calorimetry (DSC) data relating to pro-teins...
<p>The scan rate was 1.0 K/min, and the protein concentration was 10 µM. The profile shows an endoth...
Denaturation temperatures and enthalpies of bovine serumalbumin (BSA) and human serumalbumin (HSA) m...
<p>DSC thermograms of C-214-HrpZ<sub>Pss</sub> (A) and full length HrpZ<sub>Pss</sub> (B). The scan ...
Denaturation temperatures and enthalpies of bovine serumalbumin (BSA) and human serumalbumin (HSA) m...
Denaturation temperatures and enthalpies of bovine serumalbumin (BSA) and human serumalbumin (HSA) m...
<p>Heat induced unfolding curves of HPR and its variants are shown as plots of <i>f</i><sub>D</sub> ...
Thermally-induced protein unfolding is commonly described with the two-state model. This model assum...
<p>The protein concentration was 0.75 mg/ml in 30 mM sodium acetate buffer (pH 7.0). (A) ODC_WT; (B)...
<p>The GdmCl concentration was taken for 50% of the protein fraction unfolded each and melting tempe...
<p>(A): Wild type (Black) and V42M (Brown) fitted curves were obtained from cursor initiative fittin...
<p>The thermal stability of wildtype SOD1 and SOD1<sup>G93A</sup> mutants was assessed at two concen...
<p>Protein concentration was 1.3·mL<sup>−1</sup> under 50 mM buffer, either acetic/acetate at pH 4.0...
<p>*Experimental conditions were 50 mM acetic/acetate pH 4.0; 50 mM Glycine/HCl pH 2.5–3.5. The erro...
<p>Thermal unfolding curves recorded from 25 to 90°C were expressed as fraction folded derived from ...
New approaches to the analysis of differential scanning calorimetry (DSC) data relating to pro-teins...
<p>The scan rate was 1.0 K/min, and the protein concentration was 10 µM. The profile shows an endoth...
Denaturation temperatures and enthalpies of bovine serumalbumin (BSA) and human serumalbumin (HSA) m...
<p>DSC thermograms of C-214-HrpZ<sub>Pss</sub> (A) and full length HrpZ<sub>Pss</sub> (B). The scan ...
Denaturation temperatures and enthalpies of bovine serumalbumin (BSA) and human serumalbumin (HSA) m...
Denaturation temperatures and enthalpies of bovine serumalbumin (BSA) and human serumalbumin (HSA) m...
<p>Heat induced unfolding curves of HPR and its variants are shown as plots of <i>f</i><sub>D</sub> ...
Thermally-induced protein unfolding is commonly described with the two-state model. This model assum...
<p>The protein concentration was 0.75 mg/ml in 30 mM sodium acetate buffer (pH 7.0). (A) ODC_WT; (B)...
<p>The GdmCl concentration was taken for 50% of the protein fraction unfolded each and melting tempe...
<p>(A): Wild type (Black) and V42M (Brown) fitted curves were obtained from cursor initiative fittin...
<p>The thermal stability of wildtype SOD1 and SOD1<sup>G93A</sup> mutants was assessed at two concen...