Experiments were carried out in 0.1 cm quartz cell using a Jasco J-710 spectrometer with 100 μM peptide solutions (1.25% trifluoroethanol in water) at 20°C.
J 710 spectrometer
Manufactured by Jasco
The J-710 spectrometer is a laboratory instrument designed for the measurement and analysis of optical spectra. It is capable of detecting and analyzing the absorption, emission, or reflectance properties of various materials across a wide range of wavelengths.
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Lab products found in correlation
Cary 5000 uv vis nir spectrometer, by Agilent Technologies (1 mentions)
Apex duo, by Bruker (1 mentions)
Apex 2 ccd detector, by Bruker (1 mentions)
S 4700 electron microscope, by Hitachi (1 mentions)
Bx41 microscope, by Olympus (1 mentions)
Specord s600, by Analytik Jena (1 mentions)
Dc4100 driver, by Thorlabs (1 mentions)
8 protocols using j 710 spectrometer
1
Peptide Conformational Analysis by CD
2
Circular Dichroism Spectroscopy Protocol
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CD spectra were
measured by using a Jasco J-710 spectrometer. We used a temperature-controlled
quartz cuvette with a 0.2 mm path length for 1.0 mg/mL (1.0 mM) samples.
The temperature was controlled at 20 °C by an external water
bath. The CD spectra were collected at 0.2 nm intervals and averaged
over 5 scans and smoothed by the second order Savitzky-Golay method
over 15 data points.
measured by using a Jasco J-710 spectrometer. We used a temperature-controlled
quartz cuvette with a 0.2 mm path length for 1.0 mg/mL (1.0 mM) samples.
The temperature was controlled at 20 °C by an external water
bath. The CD spectra were collected at 0.2 nm intervals and averaged
over 5 scans and smoothed by the second order Savitzky-Golay method
over 15 data points.
3
Thermal Stability Characterization of ACE2 Variants
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CD data were collected on a Jasco J-710 spectrometer using purified ACE2 variant solutions in 1-mm quartz cuvettes. ACE2 variants were diluted in 300 L PBS, pH 7.4, to concentrations ranging from 2 to 3 M. Melting curves at 225 nm were measured by increasing the temperature from 25 °C to 80 °C using a rate of 1 °C per minute. CD spectra from 200 to 280 nm were measured at 25 °C and 80 °C. Melting curve data were normalized using an average of the before-melt baseline as 0% and an average of the after-melt baseline as 100%, and the apparent melting temperature, , was determined to be the temperature at which 50% of the protein was denatured between these points. Melting was irreversible for WT ACE2.
4
Circular Dichroism Analysis of HUG Polymer
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HUG was dissolved
in a concentration of 0.1 g L–1 in PBS pH = 7.4.
Circular dichroism analysis (CD) was performed with the polymer alone
and in the presence of the ligand BR. CD spectra were recorded at
25 °C in a thermostatic cell from 200 to 500 nm on a Jasco J-710
spectrometer under constant nitrogen purge. An external bath was used
for temperature control. CD data are reported as the mean molar ellipticity
[θ] of the residue in mdeg cm2 dmol–1.
in a concentration of 0.1 g L–1 in PBS pH = 7.4.
Circular dichroism analysis (CD) was performed with the polymer alone
and in the presence of the ligand BR. CD spectra were recorded at
25 °C in a thermostatic cell from 200 to 500 nm on a Jasco J-710
spectrometer under constant nitrogen purge. An external bath was used
for temperature control. CD data are reported as the mean molar ellipticity
[θ] of the residue in mdeg cm2 dmol–1.
5
Characterization of Cellulose Nanocrystal Films
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All reagents were purchased from standard suppliers and used without further purification. Aqueous suspensions of CNCs (2 wt%; pH 2.1) prepared from bleached kraft pulp were obtained from FPInnovations (Supplementary Figure 1 ). All materials for polymerization were purged with nitrogen before use. POM images were recorded on an Olympus BX41 microscope with linear polarizers. Transmission polarized UV-visible spectra were collected with an Agilent Cary 5000 UV-vis/NIR spectrometer. The sample was placed between linear polarizers, which were oriented parallel or crossed as indicated in the text and figure captions. CD spectroscopy was performed in transmission mode using a JASCO J-710 spectrometer. SEM was performed using a Hitachi S4700 electron microscope on gold sputter-coated samples. 2D-XRD images were recorded with a Bruker APEX DUO with APEX II CCD Detector using Cu Kα1 X-ray beam with a wavelength (λ) of 0.154 nm at 0.6 mA, 45 kV for 480 s at 60 mm from the detector in transmission mode. Tensile testing was performed on an Instron 5566Q at a rate of 50 mm min−1.
6
Photophysical Properties of AzoCm
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The photophysical properties of the compound azoCm were determined in 1 × PBS buffer (phosphate-buffered saline), except for the stability measurements that were carried out in HeLa cell extracts and experiments in presence of RNA which were performed in the corresponding SELEX buffer. For the UV/vis-absorption measurements, the concentrations were kept below 100 μM and the samples were prepared in UV-permeable quartz glass cuvettes with 1 cm path length. Absorption spectra were recorded using a Specord S600 or S100 spectrometer (Analytik Jena). For irradiation experiments, ThorLabs light emitting diodes (LEDs) controlled by a ThorLabs DC4100-Driver were applied. UV-light for trans-cis isomerization was provided by a λ = 365 nm LED while cis-trans isomerization was induced using a λ = 420 nm LED (type M365L2 and M420L2, 300 mW).
The CD measurements were executed with a Jasco J-710 spectrometer under constant nitrogen flow of 1.5 l/min. Here, cuvettes with 1 mm path length were used and irradiation was also carried out with the same set of ThorLabs LEDs. In these experiments, the RNA concentration was 10 μM and the ligand azoCm was provided in 10-fold excess with a concentration of 100 μM.
The CD measurements were executed with a Jasco J-710 spectrometer under constant nitrogen flow of 1.5 l/min. Here, cuvettes with 1 mm path length were used and irradiation was also carried out with the same set of ThorLabs LEDs. In these experiments, the RNA concentration was 10 μM and the ligand azoCm was provided in 10-fold excess with a concentration of 100 μM.
7
Thermal Stability Analysis of ACE2 Variants
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CD data were collected on a Jasco J-710 spectrometer using purified ACE2 variant solutions in 1 mm quartz cuvettes. ACE2 variants were diluted in 300 μl PBS, pH 7.4 to concentrations ranging from 2 to 3 μM. Melting curves at 225 nm were measured by increasing the temperature from 25 °C to 80 °C using a rate of 1 °C per minute. CD spectra from 200 to 280 nm were measured at 25 °C and 80 °C. Melting curve data were normalized using an average of the before-melt baseline as 0% and an average of the after-melt baseline as 100%, and the apparent melting temperature, Tm,app was determined to be the temperature at which 50% of the protein was denatured between these points. Melting was irreversible for WT ACE2.
8
Circular Dichroism Analysis of Protein Helicity
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Total helicity was assessed by circular dichroism (CD) as previously described (23) . The CD instrument was calibrated against camphor sulfonate primary standards according to the manufacturer's instructions before all the experiments. Spectra were acquired using a Jasco J-710 spectrometer at a protein A280 0.5 in PBS buffer (5mM sodium phosphate at pH 7.4 plus 150mM NaCl) in a 1.0 mm path cell from 190 nm to 300 nm. The resulting spectra converted into molar ellipticity, 222, using a molar extinction coefficient provided by Protparam and fit to a 3-basis model ( 25) that we and others (26) (27) (28) have used extensively for assessing STR containing proteins.
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