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Peltier device

Manufactured by Jasco
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A Peltier device is a solid-state heat pump that uses the thermoelectric effect to move heat from one side of the device to the other, creating a temperature difference. It can be used for heating, cooling, or temperature control applications.

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Lab products found in correlation

J 810 spectropolarimeter, by Jasco (3 mentions) J 815 cd spectrometer, by Jasco (2 mentions) J 815 spectropolarimeter, by Jasco (1 mentions)

6 protocols using peltier device

1

Thermal Unfolding of β2-Microglobulin Variants

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Thermal unfolding was monitored at 202 nm in the 20–95 °C range using a JASCO J-810 spectropolarimeter equipped with a Peltier device and a fluorescence detector (JASCO corporation, Tokyo, Japan). For all β2m variants involved in this study ramps were carried out in 50 mM sodium phosphate, pH 7.4. Protein concentration was set to 0.1 mg/mL (cell path 0.1 cm), and the temperature increase was 50 °C/h. Tm values were determined as the minima of the first derivative of the unfolding profiles. Thermal unfolding experiments display high reproducibility.
Le Marchand T., de Rosa M., Salvi N., Sala B.M., Andreas L.B., Barbet-Massin E., Sormanni P., Barbiroli A., Porcari R., Sousa Mota C., de Sanctis D., Bolognesi M., Emsley L., Bellotti V., Blackledge M., Camilloni C., Pintacuda G, & Ricagno S. (2018). Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity. Nature Communications, 9, 1658.
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2

Thermal Stability of β2m Mutants

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Far-UV spectra (190–260 nm) and thermal unfolding (monitored at 202 nm in the 20–95°C temperature range) for β2m D34N, D38N, D53N, D59N, D96N, D98N were measured using a JASCO J-810 spectropolarimeter equipped with a Peltier device and a fluorescence detector (JASCO corporation, Tokyo, Japan). All temperature ramps were performed in 50 mM sodium phosphate, pH 7.4, if not otherwise stated; the protein concentration was 0.1 mg/mL (cell path 0.1 cm), and the ramp slope was set at 50°C/h. Tm values were determined as the minima of the first derivative of the unfolding profiles. Thermal unfolding experiments were repeated four times for each β2m variant: the Tms shown in Fig 2C represent the average values from the four experiments, the corresponding standard deviations were also calculated.
de Rosa M., Barbiroli A., Giorgetti S., Mangione P.P., Bolognesi M, & Ricagno S. (2015). Decoding the Structural Bases of D76N ß2-Microglobulin High Amyloidogenicity through Crystallography and Asn-Scan Mutagenesis. PLoS ONE, 10(12), e0144061.
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3

Spectroscopic Analysis of BSA Oxidation

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Initially, BSA was reduced as described for PDI above. Far-UV CD spectra of 3 μM reduced BSA were recorded in 40 mM potassium phosphate (pH 7.5) at 30 °C in the presence of buffer, 150 μM H2O2, 150 μM 6-OHDA or 150 μM 6-OHDA-PEG3-yne using a Jasco J-815 spectropolarimeter. Samples were incubated with the corresponding reagents for 12–16 h at 4 °C and transferred to 30 °C 5 min before recording (data interval: 0.5 nm, cell length: 0.1 mm, 8 accumulations). The temperature during the experiment was controlled with a Jasco Peltier device.
Farzam A., Chohan K., Strmiskova M., Hewitt S.J., Park D.S., Pezacki J.P, & Özcelik D. (2019). A functionalized hydroxydopamine quinone links thiol modification to neuronal cell death. Redox Biology, 28, 101377.
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4

Thermal Stability Analysis of Rac1 Protein

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Circular dichroism data were collected on a JASCO J-815 CD spectrometer (Oklahoma City, OK, USA) with a JASCO Peltier device and water bath to control the temperature. Experiments were performed in a 1-mm cuvette at a protein concentration of 15 μM in 10 mM potassium phosphate (pH 6.5). Far-UV scans were from 200 to 280 nm. Thermal denaturation of Rac1 and Rac1 variants were monitored at 222 nm to estimate the protein melting temperature. The temperature ramp rate was 1 °C/min and data points were collected every 1 °C. All data are reported in units of mean residue ellipticity, which was calculated as follows: [θ]MRE = (θraw × MRW)/(10 × c × l), where θraw is the ellipticity in degrees, MRW is (molecular mass in kilodaltons)/(No. of residues – 1), c is the protein concentration in g/ml, and l is the pathlength of the cuvette in cm, according to [50 (link)].
Hobbs G.A., Mitchell L.E., Arrington M.E., Gunawardena H.P., DeCristo M.J., Loeser R.F., Chen X., Cox A.D, & Campbell S.L. (2014). Redox regulation of Rac1 by thiol oxidation. Free radical biology & medicine, 79, 237-250.
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5

Circular Dichroism Analysis of Protein Folding

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All circular dichroism experiments, including spectra, thermal melts, and guanidine denaturation, were conducted in ammonium acetate sample buffer. Data were collected using a JASCO J-815 CD spectrometer with temperatures controlled by a JASCO Peltier device and water bath. Data were collected using protein concentrations between 30 μM and 45 μM and either 50 μM ZnSO4 (for zinc-bound samples) or 100 μM EDTA (for apo samples). Spectra were collected by varying wavelength from 190 to 250 nm at 20°C, and thermal denaturation curves were measured at 222 nm while varying temperature from 4°C to 95°C at 2°C/min. For the chemical denaturation experiments the CD signal at 222 nm was measured at 20°C. The concentration of guanidine hydrochloride (GuHCl) was varied by mixing different ratios of protein (30 μM) prepared in 0 M or 7 M GuHCl. GuHCl concentrations were measured based on refractive index20 (link). Chemical denaturation data were fit assuming a two-state folding model and that the free energy of folding varies linearly with the concentration of GuHCl21 (link). CD spectra were analyzed with the BeStSel program to estimate helical content22 .
Guffy S.L., Pulavarti S.V., Harrison J., Fleming D., Szyperski T, & Kuhlman B. (2023). Inside-out Design of Zinc Binding Proteins with Non-native Backbones. Biochemistry, 62(3), 770-781.
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6

Measuring Protein Thermostability via CD

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The CD spectra in the far UV region (250–200 nm) of cBLS, CenACDd, and cBLS-CenACDd complexes in TBS-TC buffer were measured on a J-810 spectropolarimeter (Jasco, Tokyo, Japan) using quartz cuvettes of either 1 or 5 mm path length. The results were expressed in units of molar ellipticity (° cm2 dmolprot−1) per dmol of protein subunits.
The heat-induced denaturation of the protein samples was monitored by measuring the CD signal at 222 nm as a function of temperature. The samples were slowly heated from 20 to 95 °C at 4 °C/min using a Peltier device (Jasco, Tokyo, Japan). The molar ellipticity at 222 nm was measured every 0.5 °C. The melting temperature (Tm) of each protein was calculated from the middle point of the unfolding curve measured. Due to the irreversibility of the unfolding transitions observed at the experimental conditions used, we report apparent Tm values (Tmapp).
Iglesias Rando M.R., Gorojovsky N., Zylberman V., Goldbaum F.A, & Craig P.O. (2023). Improvement of Cellulomonas fimi endoglucanase CenA by multienzymatic display on a decameric structural scaffold. Applied Microbiology and Biotechnology.
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