<p>(A) Temperature dependence of purified wild type PpAzoR (circles), 2A1 (diamonds) and 2A1-Y179H (triangles) variants. Reactions were performed in 100 mM sodium phosphate buffer, pH 7, in the presence of 100 µM AQS and 250 µM NADPH. (B) Light scattering of wild type PpAzoR (circles), 1B6 (squares) and 2A1-Y179H (triangles) variants. (C) Thermal inactivation of wild type PpAzoR (circles) and 2A1-Y179H (triangles) variant; enzyme samples were incubated at 50°C and activity measured at 30°C in aliquots taken at different time intervals.</p
<p>Red, wild-type bglTm; blue, T1 mutant; green, T2 mutant. The stability of the wild-type bglTm pro...
<p>Enzyme activity was determined by measuring the acetolactate-formation activity of each enzyme af...
<p>A) Melting temperatures of DhaA wild-type (blue) and DhaA115 (red) in the presence of indicated s...
<p>(A) Activity remaining at 30°C following heating to the indicated temperature for 1 h of wild typ...
<p>Wild type PpAzoR (circles), B1G6 from 1<sup>st</sup> generation (squares), 16B7 from 2<sup>nd</su...
<p>Thermal stability of the PGK1 wild-type and variants at 45°C (panel A) and at 37°C (panel B). Eac...
<p>(A) Thermal stability of WT and mutant CKs: WT (square), H26Y (circle), P36T (triangle) and K267E...
<p>Plots of the residual activities at 10 min incubation <i>vs.</i> temperature. The enzyme solution...
<p>(A) Temperature dependence of kinase activity of PGK1 wild type and variants. (B) Non-linear fit ...
<p>(A) The relative enzyme activity was assayed by d-tagatose formation for 30 min. Activity at the ...
<p>Temperature-induced changes in CD ellipticity at 222 nm were measured at increasing concentration...
<p>(A) and (B) Illustrative plots of activity versus time for experiments performed at several tempe...
Protein stability arises from a combination of factors which are often difficult to rationalise. The...
<p>The thermal denaturation of the enzyme (0.25 mg/ml) in the non-salt buffer was monitored by chang...
<p>(<b>A</b>) Pim-1 wild type and mutants were heated from 10°C to 72°C in a 0.1-cm quartz cuvette a...
<p>Red, wild-type bglTm; blue, T1 mutant; green, T2 mutant. The stability of the wild-type bglTm pro...
<p>Enzyme activity was determined by measuring the acetolactate-formation activity of each enzyme af...
<p>A) Melting temperatures of DhaA wild-type (blue) and DhaA115 (red) in the presence of indicated s...
<p>(A) Activity remaining at 30°C following heating to the indicated temperature for 1 h of wild typ...
<p>Wild type PpAzoR (circles), B1G6 from 1<sup>st</sup> generation (squares), 16B7 from 2<sup>nd</su...
<p>Thermal stability of the PGK1 wild-type and variants at 45°C (panel A) and at 37°C (panel B). Eac...
<p>(A) Thermal stability of WT and mutant CKs: WT (square), H26Y (circle), P36T (triangle) and K267E...
<p>Plots of the residual activities at 10 min incubation <i>vs.</i> temperature. The enzyme solution...
<p>(A) Temperature dependence of kinase activity of PGK1 wild type and variants. (B) Non-linear fit ...
<p>(A) The relative enzyme activity was assayed by d-tagatose formation for 30 min. Activity at the ...
<p>Temperature-induced changes in CD ellipticity at 222 nm were measured at increasing concentration...
<p>(A) and (B) Illustrative plots of activity versus time for experiments performed at several tempe...
Protein stability arises from a combination of factors which are often difficult to rationalise. The...
<p>The thermal denaturation of the enzyme (0.25 mg/ml) in the non-salt buffer was monitored by chang...
<p>(<b>A</b>) Pim-1 wild type and mutants were heated from 10°C to 72°C in a 0.1-cm quartz cuvette a...
<p>Red, wild-type bglTm; blue, T1 mutant; green, T2 mutant. The stability of the wild-type bglTm pro...
<p>Enzyme activity was determined by measuring the acetolactate-formation activity of each enzyme af...
<p>A) Melting temperatures of DhaA wild-type (blue) and DhaA115 (red) in the presence of indicated s...