<p>Protein samples (0.3 mg/ml) in buffer F (20 mM HEPES/NaOH pH 7.5, containing 100 mM NaCl and 2 mM DTT) were heated with a rate of 1°C/min in the range of 20–85°C. The data presented are mean values of four measurements with error bars corresponding to standard deviation.</p
<p><b>A.</b> Wild-type (WT) FHbp ID 1 (dashed grey line) and Q38R mutant (solid black line). <b>B-E....
<p>The thermal unfolding of 0.1 mg/mL of WT and deamidated TIMs was monitored by recording the chang...
a<p>(M<sup>−1</sup>s<sup>−1</sup> (×10<sup>5</sup>).</p>b<p>Melting temperature (T<sub>m</sub> in °C...
<p>(A): Wild type (Black) and V42M (Brown) fitted curves were obtained from cursor initiative fittin...
<p>A) Protein samples were incubated at different temperatures for 30 minutes and the remaining fluo...
<p><i>A,</i> Near- and <i>B,</i> Far-UV CD spectra of wild-type and mutant αB-crystallin proteins. S...
<p>The protein samples (750 µg) were incubated in 1 ml PO4 buffer, pH 7.2 at 43°C and light scatteri...
<p>Far-UV CD spectra <b>(A)</b> and near-UV spectra <b>(B)</b> of HSP18 at different temperatures (2...
<p>Effect of temperature on aggregation. <b>A)</b> Light scattered intensity at 90° angle registered...
Effect of temperature, varying from 20 to 45°C, on the oligomeric forms of the H. volcanii S-layer p...
<p>Protein samples (0.1 mg/ml) in buffer FF (50 mM phosphate (pH 7.5) containing 100 mM NaCl and 15 ...
<p>Protein stability was analyzed in 12 different pH buffers in four independent measurements. (A) H...
Increase in fluorescence was detected as hydrophobic regions of the protein were exposed as the prot...
<p>The scan rate were 0.5 K/min (short dashed line), 0.75 K/min (solid line), 1.0 K/min (dash dotted...
New methods and tools (I), Poster Session, Abstract, Meeting Program of EABS & BSJ 200
<p><b>A.</b> Wild-type (WT) FHbp ID 1 (dashed grey line) and Q38R mutant (solid black line). <b>B-E....
<p>The thermal unfolding of 0.1 mg/mL of WT and deamidated TIMs was monitored by recording the chang...
a<p>(M<sup>−1</sup>s<sup>−1</sup> (×10<sup>5</sup>).</p>b<p>Melting temperature (T<sub>m</sub> in °C...
<p>(A): Wild type (Black) and V42M (Brown) fitted curves were obtained from cursor initiative fittin...
<p>A) Protein samples were incubated at different temperatures for 30 minutes and the remaining fluo...
<p><i>A,</i> Near- and <i>B,</i> Far-UV CD spectra of wild-type and mutant αB-crystallin proteins. S...
<p>The protein samples (750 µg) were incubated in 1 ml PO4 buffer, pH 7.2 at 43°C and light scatteri...
<p>Far-UV CD spectra <b>(A)</b> and near-UV spectra <b>(B)</b> of HSP18 at different temperatures (2...
<p>Effect of temperature on aggregation. <b>A)</b> Light scattered intensity at 90° angle registered...
Effect of temperature, varying from 20 to 45°C, on the oligomeric forms of the H. volcanii S-layer p...
<p>Protein samples (0.1 mg/ml) in buffer FF (50 mM phosphate (pH 7.5) containing 100 mM NaCl and 15 ...
<p>Protein stability was analyzed in 12 different pH buffers in four independent measurements. (A) H...
Increase in fluorescence was detected as hydrophobic regions of the protein were exposed as the prot...
<p>The scan rate were 0.5 K/min (short dashed line), 0.75 K/min (solid line), 1.0 K/min (dash dotted...
New methods and tools (I), Poster Session, Abstract, Meeting Program of EABS & BSJ 200
<p><b>A.</b> Wild-type (WT) FHbp ID 1 (dashed grey line) and Q38R mutant (solid black line). <b>B-E....
<p>The thermal unfolding of 0.1 mg/mL of WT and deamidated TIMs was monitored by recording the chang...
a<p>(M<sup>−1</sup>s<sup>−1</sup> (×10<sup>5</sup>).</p>b<p>Melting temperature (T<sub>m</sub> in °C...