The 1H NMR spectra were recorded at 298 K on a Varian Unity Inova 500 MHz instrument. A PerkinElmer Spectrum-One FT-IR was employed to monitor the IR spectra of the reported complexes. UV–vis spectra were obtained with a Varian Cary 50 UV–vis spectro-photometer. Luminescence spectra were recorded with a Cary Eclipse Spectrometer. Microanalyses (C, H, and N) were performed using a PerkinElmer 2400 Series II elemental analyzer. Cyclic voltammograms were recorded with a CH Instruments electrochemistry system using Pt electrode, and tetraethylammonium perchlorate as supporting electrolyte. X-band electron paramagnetic resonance (EPR) spectra were recorded with a Bruker EMX Spectrometer.
Eclipse spectrometer
Manufactured by Agilent Technologies
The Eclipse spectrometer is a compact and high-performance analytical instrument designed for laboratory use. It provides accurate and reliable spectroscopic measurements across a wide range of wavelengths, enabling precise analysis and identification of various chemical compounds and materials.
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Lab products found in correlation
Emx spectrometer, by Bruker (1 mentions)
Unity inova 500 mhz instrument, by Agilent Technologies (1 mentions)
Cary 50 uv vis spectrophotometer, by Agilent Technologies (1 mentions)
2400 series 2, by PerkinElmer (1 mentions)
Spectrum one ftir, by PerkinElmer (1 mentions)
Pd minitrap g 25 column, by Cytiva (1 mentions)
Uv 1800, by Shimadzu (1 mentions)
D8 venture diffractometer, by Bruker (1 mentions)
Avance 3 500 spectrometer, by Bruker (1 mentions)
Fluorolog 3 22, by Horiba (1 mentions)
6 protocols using eclipse spectrometer
1
Comprehensive Spectroscopic Characterization
2
Studying Gα Subunit Activation Kinetics
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GαS and GαS variants were exchanged into buffer containing 20 mM HEPES pH 8.0, 150 mM NaCl, and 5 μM GDP using a PD MiniTrap G25 column (Cytiva), and the sample volumes were adjusted to achieve a final concentration of 10 μM protein. Tryptophan fluorescence spectra were recorded with a Cary Eclipse spectrometer operating at 25 °C. The excitation wavelength was 280 nm and emission was observed at 340 nm with 5 nm excitation and emission bandwidths. GTPγS was added to 200 μL protein for a final concentration of 50 μM in a quartz cuvette. The sample was mixed vigorously by repeated pipetting and data collection immediately started. Data points were recorded every 12 seconds for 200 minutes total acquisition time. Data were analyzed in GraphPad prism using the one-phase association equation shown below:
where is the fluorescence intensity when (time) equals zero, ‘Plateau’ is the fluorescence intensity when the system has been fully equilibrated at infinite time expressed in the same units as , and is the rate constant, expressed as the reciprocal of the x-axis time units.
where is the fluorescence intensity when (time) equals zero, ‘Plateau’ is the fluorescence intensity when the system has been fully equilibrated at infinite time expressed in the same units as , and is the rate constant, expressed as the reciprocal of the x-axis time units.
3
Spectrophotometric and Fluorescence Analysis
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The samples were analysed using a UV-1800-Shimadzu spectrophotometer with quartz cells of 1 cm path length with the corresponding buffer as reference for the measurements. The steady state fluorescence spectroscopy measurements were performed using a Cary Eclipse Spectrometer with λex = 280 nm.
4
Rapid Cu2+ Binding Kinetics of SUP
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A sample of SUP was diluted in HEPES buffer (20 mM, pH 7.4) containing 100 mM NaCl to a final concentration of 5 μM. Increasing amounts of a 1 mM stock solution of CuSO4 were added to the sample, and fluorescence emission spectra were immediately recorded on a Cary Eclipse spectrometer at RT (λexc = 260 nm, λem = 290–400 nm, slits 5 nm) using a 10 × 4 mm quartz cuvette. Recording spectra after various equilibration times (min to h) did not show any variation in signal intensity, indicating that the binding of Cu2+ was rapid. Data presented is the average of three independent titrations.
5
Structural and Optical Characterization of Molecular Complexes
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X-ray diffraction measurements were made at 133 K on a Bruker D8 Venture diffractometer with a microfocus sealed tube and a Photon II detector using graphite monochromated Mo-Kα radiation (λ = 0.71073 Å). NMR spectra were recorded on a Bruker Avance III 500 spectrometer at 500 MHz for 1H and 125.7 MHz for 13C. Lifetime measurements and photoluminescence measurements of the complexes were made on a Cary Eclipse spectrometer with a xenon lamp as an excitation source, as well as on an N-400M fluorescent microscope. The quantum yields and photoluminescence measurements are performed at FluoroLog3-22, Horiba JobinYvon equipped with an integration sphere.
The crystal structure was solved by direct methods using SHELXT [41 (link)] and was refined by full-matrix least-squares calculations on F2 (SHELXL2018 [42 (link)]) in the graphical user interface Shelxle [43 (link)]. The molecular structure is represented using Mercury v4.0 software [44 (link)]. The CIE 1931 chromatograms were obtained using the LED ColorCalculator v7.77 [45 ].
The crystal structure was solved by direct methods using SHELXT [41 (link)] and was refined by full-matrix least-squares calculations on F2 (SHELXL2018 [42 (link)]) in the graphical user interface Shelxle [43 (link)]. The molecular structure is represented using Mercury v4.0 software [44 (link)]. The CIE 1931 chromatograms were obtained using the LED ColorCalculator v7.77 [45 ].
6
ApoA-I Heparin Interaction Fluorescence
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ApoA-I at 18 µM at pH 4 and pH 7, in the absence and presence of heparin (36 µM), were incubated at 37 °C with agitation. Fluorescence spectra from 300 to 400 nm were collected on a Cary Eclipse spectrometer, with excitation at 279 nm and a band pass of 1 nm, immediately and 1 hour after preparation of the samples.
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