Raw DSC thermograms show changes in the molar heat capacity of MsEis (Panel A) and RvEis (Panel B) proteins at increasing temperature from 20°C to 110°C. The protein concentration was 0.25 mg/ml for each experiment. The transition curve in both the cases is shown after the subtraction of buffer reference and normalization with the concentration used for measurement. Inset shows the zoomed view of endothermic peak of RvEis.</p
<p>(A) Thermal stability of DTT and DTNF proteins measured by DSC. Left panel, temperature dependent...
New approaches to the analysis of differential scanning calorimetry (DSC) data relating to pro-teins...
<p>(A) Thermograms (scan 1) of 0.2 and 0.3 mg·mL<sup>-1</sup> protein (solid lines) and 0.6 mg·mL<su...
Raw DSC thermograms of MsEis (Panel A) and RvEis (Panel B) after subtraction of buffer baseline and ...
Intrinsic tryptophan fluorescence spectra of MsEis and RvEis proteins in the presence of increasing ...
Size Exclusion Chromatographic (SEC) elution profiles of MsEis (Panel A) and RvEis (Panel B) protein...
(Panel A) A characteristic Far-UV CD spectra of MsEis was recorded in 20 mM phosphate buffer, pH 8.0...
<p>The temperature dependencies of excess specific heat capacity for rWT L35Ae and L35Ae 10X, fitted...
<p>Four representative experiments are shown, one for each MSPβ: Wild-type glycosylated, wild-type d...
<p>A) Profiles of apparent molar heat capacities (<i>C</i>p<sub>app</sub>) <i>vs</i> temperature (<i...
The thermal denaturation of S-protein is investigated at pH 7.0 by means of DSC measurements. The p...
The thermal denaturation of S-protein is investigated at pH 7.0 by means of DSC measurements. The p...
The thermal denaturation of S-protein is investigated at pH 7.0 by means of DSC measurements. The p...
This thesis aims at understanding the molecular origins of urea-induced protein denaturation, in par...
<p>DSC thermograms of C-214-HrpZ<sub>Pss</sub> (A) and full length HrpZ<sub>Pss</sub> (B). The scan ...
<p>(A) Thermal stability of DTT and DTNF proteins measured by DSC. Left panel, temperature dependent...
New approaches to the analysis of differential scanning calorimetry (DSC) data relating to pro-teins...
<p>(A) Thermograms (scan 1) of 0.2 and 0.3 mg·mL<sup>-1</sup> protein (solid lines) and 0.6 mg·mL<su...
Raw DSC thermograms of MsEis (Panel A) and RvEis (Panel B) after subtraction of buffer baseline and ...
Intrinsic tryptophan fluorescence spectra of MsEis and RvEis proteins in the presence of increasing ...
Size Exclusion Chromatographic (SEC) elution profiles of MsEis (Panel A) and RvEis (Panel B) protein...
(Panel A) A characteristic Far-UV CD spectra of MsEis was recorded in 20 mM phosphate buffer, pH 8.0...
<p>The temperature dependencies of excess specific heat capacity for rWT L35Ae and L35Ae 10X, fitted...
<p>Four representative experiments are shown, one for each MSPβ: Wild-type glycosylated, wild-type d...
<p>A) Profiles of apparent molar heat capacities (<i>C</i>p<sub>app</sub>) <i>vs</i> temperature (<i...
The thermal denaturation of S-protein is investigated at pH 7.0 by means of DSC measurements. The p...
The thermal denaturation of S-protein is investigated at pH 7.0 by means of DSC measurements. The p...
The thermal denaturation of S-protein is investigated at pH 7.0 by means of DSC measurements. The p...
This thesis aims at understanding the molecular origins of urea-induced protein denaturation, in par...
<p>DSC thermograms of C-214-HrpZ<sub>Pss</sub> (A) and full length HrpZ<sub>Pss</sub> (B). The scan ...
<p>(A) Thermal stability of DTT and DTNF proteins measured by DSC. Left panel, temperature dependent...
New approaches to the analysis of differential scanning calorimetry (DSC) data relating to pro-teins...
<p>(A) Thermograms (scan 1) of 0.2 and 0.3 mg·mL<sup>-1</sup> protein (solid lines) and 0.6 mg·mL<su...