<p>(A) Kinetics of thermal inactivation experiments probing dynamics of heat-induced loss of function. Wild-type and variant MCAD proteins were incubated at indicated temperatures and residual activity was plotted as a function of incubation time. (B) Arrhenius Plots resulting from kinetic constants <i>k</i> of time-dependent thermal denaturation experiments. (C) Activation energies (E<sub>A</sub>) calculated from Arrhenius Plots reflect the energy barrier between the conformational state with full residual activity and the non-active state after application of thermal stress.</p
<p>A) Temperature dependence of denaturation enthalpies (Δ<i>H</i>) for holo- (closed symbols) and a...
<p>(A) Thermal stability of WT and mutant CKs: WT (square), H26Y (circle), P36T (triangle) and K267E...
Traditionally, the dependence of enzyme activity on temperature has been described by a model consis...
Heat induced enzyme inactivation or protein denaturation is now well documented, due to progresses i...
<p>(A) and (B) Illustrative plots of activity versus time for experiments performed at several tempe...
<p>Heat inactivation kinetic constants and the derived half-life for the thermal unfolding process o...
<p>The kinetics of heat inactivation of the extracellular proteinase from <em>Pseudomona...
<p>Heat activation is visible at pH(circles, solid line), 9 (squares, broken line) and 10 (triangles...
<p>Red, wild-type bglTm; blue, T1 mutant; green, T2 mutant. The stability of the wild-type bglTm pro...
The kinetics of heat inactivation of the extracellular proteinase from Pseudomonas fluorescens 22F w...
a<p>determined at 3°C/min scan rate.</p>b<p>mean±s.d. from independent experiments performed at thre...
<p>Activation parameters derived from the temperature dependence of intact and truncated protein-ssD...
<p>A: Effect of temperature on the activity of mutant enzymes. B: Effect of temperature on the stabi...
<p>*Calculated from the exponential decay phase in <a href="http://www.plosone.org/article/info:doi/...
New approaches to the analysis of differential scanning calorimetry (DSC) data relating to pro-teins...
<p>A) Temperature dependence of denaturation enthalpies (Δ<i>H</i>) for holo- (closed symbols) and a...
<p>(A) Thermal stability of WT and mutant CKs: WT (square), H26Y (circle), P36T (triangle) and K267E...
Traditionally, the dependence of enzyme activity on temperature has been described by a model consis...
Heat induced enzyme inactivation or protein denaturation is now well documented, due to progresses i...
<p>(A) and (B) Illustrative plots of activity versus time for experiments performed at several tempe...
<p>Heat inactivation kinetic constants and the derived half-life for the thermal unfolding process o...
<p>The kinetics of heat inactivation of the extracellular proteinase from <em>Pseudomona...
<p>Heat activation is visible at pH(circles, solid line), 9 (squares, broken line) and 10 (triangles...
<p>Red, wild-type bglTm; blue, T1 mutant; green, T2 mutant. The stability of the wild-type bglTm pro...
The kinetics of heat inactivation of the extracellular proteinase from Pseudomonas fluorescens 22F w...
a<p>determined at 3°C/min scan rate.</p>b<p>mean±s.d. from independent experiments performed at thre...
<p>Activation parameters derived from the temperature dependence of intact and truncated protein-ssD...
<p>A: Effect of temperature on the activity of mutant enzymes. B: Effect of temperature on the stabi...
<p>*Calculated from the exponential decay phase in <a href="http://www.plosone.org/article/info:doi/...
New approaches to the analysis of differential scanning calorimetry (DSC) data relating to pro-teins...
<p>A) Temperature dependence of denaturation enthalpies (Δ<i>H</i>) for holo- (closed symbols) and a...
<p>(A) Thermal stability of WT and mutant CKs: WT (square), H26Y (circle), P36T (triangle) and K267E...
Traditionally, the dependence of enzyme activity on temperature has been described by a model consis...