Differential scanning calorimetric (DSC) measurements were performed using a VP capillary DSC microcalorimeter from MicroCal with a cell volume of 137 μl. The measurements were controlled by the VP viewer program, and the instrument was equipped with an autosampler for 96-well plates. Samples were analyzed using a programmed heating scan rate of 60 °C h−1 over a temperature range from 20 to 100 °C, and cell pressure was ∼60 psi (4.136 bar). DSC thermograms were corrected for buffer baseline and protein concentration. The conditions were: 14.3 μm recombinant proMPO or 8.1 μm mature leukocyte MPO in PBS buffer, pH 7.4. For data analysis and conversion, MicroCal Origin software was used. Heat capacity (Cp) was expressed in kcal mol−1 K−1. Data points were fitted to non-two-state equilibrium-unfolding models by the Levenberg-Marquardt nonlinear least squares method.
Vp capillary dsc microcalorimeter
Manufactured by Malvern Panalytical
The VP-capillary DSC microcalorimeter is a laboratory instrument designed for high-precision measurement of heat flow. It is capable of detecting and analyzing thermal events in small samples with a high degree of sensitivity.
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5 protocols using vp capillary dsc microcalorimeter
1
Differential Scanning Calorimetry of Myeloperoxidase
2
DSC Analysis of NdCld Unfolding Thermodynamics
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Differential scanning calorimetric (DSC) measurements were performed using a VP-capillary DSC microcalorimeter from Microcal with a cell volume of 137 μl. The measurements were controlled by the VP-viewer program and the instrument was equipped with an autosampler for 96-well plates. Samples were analysed using a programmed heating scan rate of 60°C·h−1 over a temperature range from 20 to 120°C, cell pressure was approximately 60 psi (4.136 bar). DSC thermograms were corrected for buffer baseline and protein concentration. 5 μM of NdCld wild-type, E210A and K141E in 50 mM MES buffer, pH 5.5, was used for each measurement. The ligands were present in high excess (200 mM F−, 10 mM SCN−). For data analysis and conversion, the Microcal origin software was used. Heat capacity (Cp) was expressed in kcal·mol−1·K−1. Data points were fitted to non-two state equilibrium-unfolding models by the Lavenberg/Marquardt (LM) non-linear least squares method.
3
Thermal Unfolding of Proteins
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Temperature-induced pH-dependent protein unfolding studies were performed using DSC. All samples were analyzed between 20 and 100 °C. Samples were heated at 60 psi (4.136 bar) with a rate of 60 °C h−1 cell pressure using a VP-capillary DSC microcalorimeter from Microcal (cell volume: 137 μl), equipped with an autosampler for 96-well plates. All samples consisted of 10 μm enzyme in 50 mm phosphate–citrate buffer, pH 3.0–7.5 (WT) and pH 4.5–7.5 (variants) and were kept at 4 °C before measurement. Collected data were corrected for buffer baseline, normalized for protein concentration, and analyzed using the Microcal Origin software package.
4
Thermal Stability Analysis of HemQ Proteins
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Differential
scanning calorimetry (DSC) measurements were performed using a VP-capillary
DSC microcalorimeter from Microcal with a cell volume of 137 μL.
The measurements were controlled by the VP-viewer program, and the
instrument was equipped with an autosampler for 96-well plates. Samples
were analyzed using a programmed heating scan rate of 60 °C h–1 over a temperature range from 20 to 100 °C,
and the cell pressure was approximately 60 psi (4.136 bar). DSC thermograms
were corrected for buffer baseline and protein concentration. Apo-,
heme b-, or coproheme-LmHemQ and SaHemQ (5 μM
each) in 50 mM phosphate buffer (pH 7.0) were used for each measurement.
For data analysis and conversion, the Microcal origin software was
used. Heat capacity (Cp) was expressed in kilocalories per mole per kelvin. Data points
were fitted to non-two-state equilibrium unfolding models by the Lavenberg–Marquardt
(LM) nonlinear least-squares method.
scanning calorimetry (DSC) measurements were performed using a VP-capillary
DSC microcalorimeter from Microcal with a cell volume of 137 μL.
The measurements were controlled by the VP-viewer program, and the
instrument was equipped with an autosampler for 96-well plates. Samples
were analyzed using a programmed heating scan rate of 60 °C h–1 over a temperature range from 20 to 100 °C,
and the cell pressure was approximately 60 psi (4.136 bar). DSC thermograms
were corrected for buffer baseline and protein concentration. Apo-,
heme b-, or coproheme-LmHemQ and SaHemQ (5 μM
each) in 50 mM phosphate buffer (pH 7.0) were used for each measurement.
For data analysis and conversion, the Microcal origin software was
used. Heat capacity (Cp) was expressed in kilocalories per mole per kelvin. Data points
were fitted to non-two-state equilibrium unfolding models by the Lavenberg–Marquardt
(LM) nonlinear least-squares method.
5
Thermal Stability Analysis of MPO
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Differential scanning calorimetric (DSC) measurements were performed using a VP-capillary DSC microcalorimeter from Microcal (cell volume: 137 μL), controlled by the VP-viewer program and equipped with an autosampler for 96 well plates. Samples were analyzed using a programmed heating scan rate of 60 °C h− 1 over a temperature range of 20 °C to 110 °C and a cell pressure of approximately 60 psi (4.136 bar). Collected DSC data were corrected for buffer baseline and normalized for protein concentration. The reaction conditions were: 5 μM MPO in 100 mM phosphate buffer pH 5.0 in the absence or presence of 25 μM chlorite and different incubation times. Reactions were stopped by addition of 4 mM cysteine. Guanidinium hydrochloride (GdnHCl; 5 mM) was added before measurements were started to avoid non-specific protein aggregation at increasing temperatures.
Microcal origin software was used for data analysis. Heat capacity (Cp) was expressed in kcal mol− 1 K− 1 (1 cal = 4.184 J). Data points were fitted to non-two-state equilibrium-unfolding models by the Lavenberg/Marquardt (LM) non-linear least square method.
Microcal origin software was used for data analysis. Heat capacity (Cp) was expressed in kcal mol− 1 K− 1 (1 cal = 4.184 J). Data points were fitted to non-two-state equilibrium-unfolding models by the Lavenberg/Marquardt (LM) non-linear least square method.
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