where A is the absorbance, c is the molar concentration, l is the path length of the cuvette in cm, and ε is the molar absorption coefficient (M−1 cm−1). All spectral measurements were taken in triplicate.
Etcs 761
The ETCS-761 is a laboratory equipment product designed for specific functions. It has a core function of providing a controlled environment for various scientific applications. The detailed specifications and intended use of this product are not available in this concise and unbiased description.
Lab products found in correlation
14 protocols using etcs 761
Spectral Characterization of Protein Samples
where A is the absorbance, c is the molar concentration, l is the path length of the cuvette in cm, and ε is the molar absorption coefficient (M−1 cm−1). All spectral measurements were taken in triplicate.
Temperature-Dependent Carbonic Anhydrase Aggregation
where I is the light scattering intensity at temperature T, If is the limiting value of light scattering at higher temperatures. Tagg is the temperature corresponding to the middle point of the transition, i.e., a temperature at which I = If/2 and b is constant. Each curve was independently analyzed for the respective aggregation parameters and mean was calculated. The deviations (standard error) from the mean was then analyzed.
UV-vis Spectral Measurements of Protein
Spectroscopic Analysis of G-Quadruplex Folding
UV-melting analysis was performed using the Jasco V-750 UV-visible spectrophotometer equipped with a Peltier temperature control system (ETCS-761) (Jasco, JP). The spectra were analyzed with Spectra Manager (Jasco, JP). Oligonucleotides (5 μM) were annealed in 100 mM KCl, 50 mM Na-cacodylate pH 7.4 (10 min at 95°C, overnight at room temperature). The melting curves were recorded at 295 nm in a 0.5 cm path length quartz cuvette heating (20–90°C) and cooling (90–20°C) at a rate of 0.5°C/min. The thermodynamic parameters for the folding of the wild-type and modified oligonucleotides into G4 were obtained from the UV-melting curves. The ‘DNA-Melting Analysis’ program (Jasco, JP), which analyzed the melting curves according to a standard all-or-none model, gave the ΔH ° and ΔS° values. The free energy of quadruplex formation was calculated according to: ΔG ° = −RT ln K = ΔH ° − TΔS °.
Thermal and Structural Analysis of Oligonucleotides
Circular Dichroism (CD) spectra were obtained on a JASCO J-600 spectropolarimeter, equipped with a thermostated cell holder, with 5 μM oligonucleotide solutions in 50 mM Na-cacodylate, pH 7.4, 100 mM KCl. The spectra were recorded in 0.5 cm quartz cuvette at 25 and 95 °C and reported as ellipticity (mdeg) versus wavelength (nm). Each spectrum was smoothed and subtracted to the baseline.
UV-vis Spectrophotometer Characterization
UV Spectroscopy of Oligonucleotide Thermal Denaturation
Thermal Denaturation of Proteins
a JASCO UV-660 UV/Vis spectrophotometer where the temperature was
controlled by a programmable Peltier-type (ETCS-761) temperature controller
interfaced with a personal computer. Then, 4 μM protein solution
was heated at a rate of 1 °C/min from 20 to 85 °C by placing
the cuvette in the cell holder attached to the Peltier-type temperature
controller. The protein solution was heated to a temperature just
a few degrees above the temperature where complete denaturation was
achieved and then cooled back to 25 °C. This was done to check
the reversibility of thermal denaturation curves. The optical properties
were measured again and compared with those of the native protein.
Each measurement was carried out at least three times, and the baseline
was corrected by the buffer in question.
Characterization of Organic Polymers
UV Melting Experiments of Oligonucleotides
were carried out on a Jasco V-630 spectrometer equipped with a programmable
temperature-control unit (Jasco ETCS-761) using a 0.1 cm quartz cell
unless otherwise noted. The melting temperatures (Tms) were determined from the maximum in the first derivatives
of the melting curves (absorbance at 260 nm against temperature, 0.5
°C/min). Oligonucleotides were diluted at a final concentration
of 10 μM in aqueous buffers.
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