<p>The thermal stability of wildtype SOD1 and SOD1<sup>G93A</sup> mutants was assessed at two concentrations (11µM and 33µM) and in the metallated and demetallated form (when incubated with 20mM EDTA which functioned as a heavy metal chelator). Protein stability is expressed as apparent Tm, which refers to the mid-point temperature (°C) where the ratio of unfolded to folded proteins is 1∶1. Apparent Tm values reported are the average values±SD obtained from n = 3. Asterisks denote p-values calculated using the two-tailed Student t-test for the paired condition of metallated versus demetallated SOD1, where ** = p<0.005 and *** = p<10<sup>−5</sup>.</p
We report the thermal stability of wild type (WT) and 14 different variants of human copper/zinc sup...
<p>Protein thermostability has been the focus of growing research interests in the last decades sinc...
<p>(A) Thermal stability of WT and mutant CKs: WT (square), H26Y (circle), P36T (triangle) and K267E...
<p>Protein stability was analyzed in 12 different pH buffers in four independent measurements. (A) H...
<p>The temperature dependence of excess molar heat capacity of the wild-type <i>Mt</i>-NDPK (in red)...
<p>Red, wild-type bglTm; blue, T1 mutant; green, T2 mutant. The stability of the wild-type bglTm pro...
<p><b>A</b>, Representative melting curves for three mutant enzymes. The thermofluor assay was perfo...
<p>Thermal unfolding curves recorded from 25 to 90°C were expressed as fraction folded derived from ...
<p>. Stock enzyme solutions were diluted to 250 µg/ml in storage buffer containing 30% glycerol, 50 ...
<p>Four representative experiments are shown, one for each MSPβ: Wild-type glycosylated, wild-type d...
We report the thermal stability of wild type (WT) and 14 different variants of human copper/zinc sup...
<p>Experimental conditions were 50/acetate at pH 4.0 or glycine/HCl at the other pH values. Experime...
<p><b>A.</b> Wild-type (WT) FHbp ID 1 (dashed grey line) and Q38R mutant (solid black line). <b>B-E....
Engineering proteins to enhance thermal stability is a widely utilized approach for creating industr...
<p><i>A,</i> Near- and <i>B,</i> Far-UV CD spectra of wild-type and mutant αB-crystallin proteins. S...
We report the thermal stability of wild type (WT) and 14 different variants of human copper/zinc sup...
<p>Protein thermostability has been the focus of growing research interests in the last decades sinc...
<p>(A) Thermal stability of WT and mutant CKs: WT (square), H26Y (circle), P36T (triangle) and K267E...
<p>Protein stability was analyzed in 12 different pH buffers in four independent measurements. (A) H...
<p>The temperature dependence of excess molar heat capacity of the wild-type <i>Mt</i>-NDPK (in red)...
<p>Red, wild-type bglTm; blue, T1 mutant; green, T2 mutant. The stability of the wild-type bglTm pro...
<p><b>A</b>, Representative melting curves for three mutant enzymes. The thermofluor assay was perfo...
<p>Thermal unfolding curves recorded from 25 to 90°C were expressed as fraction folded derived from ...
<p>. Stock enzyme solutions were diluted to 250 µg/ml in storage buffer containing 30% glycerol, 50 ...
<p>Four representative experiments are shown, one for each MSPβ: Wild-type glycosylated, wild-type d...
We report the thermal stability of wild type (WT) and 14 different variants of human copper/zinc sup...
<p>Experimental conditions were 50/acetate at pH 4.0 or glycine/HCl at the other pH values. Experime...
<p><b>A.</b> Wild-type (WT) FHbp ID 1 (dashed grey line) and Q38R mutant (solid black line). <b>B-E....
Engineering proteins to enhance thermal stability is a widely utilized approach for creating industr...
<p><i>A,</i> Near- and <i>B,</i> Far-UV CD spectra of wild-type and mutant αB-crystallin proteins. S...
We report the thermal stability of wild type (WT) and 14 different variants of human copper/zinc sup...
<p>Protein thermostability has been the focus of growing research interests in the last decades sinc...
<p>(A) Thermal stability of WT and mutant CKs: WT (square), H26Y (circle), P36T (triangle) and K267E...