The cylindrical polymer brushes and the unlabeled core-crosslinked micelles were analyzed by multi-angle DLS. For the measurements, cylindrical quartz cuvettes (Hellma, Mühlheim, Germany) were cleaned with dust-free distilled acetone and transferred to a dust free flow box. Solutions were filtered into the cuvettes through Pall GHP filters, 0.2 μm pore size. DLS measurements were performed by the following instrument at 20 °C. The apparatus consists of a Uniphase He/Ne Laser (22.5 mW output power at λ = 632.8 nm), an ALV/SP125 goniometer with an ALV 5000/E/PCI correlator and an ALV/High QEAPD Avalanche photodiode detector. The correlation functions of the particles were fitted using a sum of two exponentials. The z-average diffusion coefficient Dz was calculated by extrapolating Dapp for q = 0. By formal application of Stokes law, the inverse z-average hydrodynamic radius is Rh = 〈Rh−1〉z−1.
Cylindrical quartz cuvette
Manufactured by Hellma
Sourced in Germany
The Cylindrical quartz cuvette is a laboratory equipment designed for spectroscopic analysis. It is made of quartz, a material known for its high optical transparency. The cuvette has a cylindrical shape, which allows for uniform light exposure of the sample during analysis.
Automatically generated - may contain errors
Lab products found in correlation
Direct detect infrared spectrometer, by Merck Group (2 mentions)
Milli q water, by Merck Group (1 mentions)
J 715 spectropolarimeter, by Jasco (1 mentions)
Pd minitrap g 25 column, by GE Healthcare (1 mentions)
Pd mini trap, by Cytiva (1 mentions)
715 spectropolarimeter, by Jasco (1 mentions)
J 715, by Jasco (1 mentions)
J 710 spectropolarimeter, by Jasco (1 mentions)
9 protocols using cylindrical quartz cuvette
1
Multi-Angle Dynamic Light Scattering
2
SANS Measurements Using EQ-SANS Instrument
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SANS measurements
were made using the EQ-SANS instrument at the Spallation Neutron Source
of Oak Ridge National Laboratory.49 (link) A single
configuration was used for all measurements. A sample-to-detector
distance of 4 m was employed with a minimum wavelength setting of
2.5 Å. The choppers ran at 30 Hz in the “frame-skipping”
mode. As a result, the wavelength bands were 2.5–6.1 Å
and 9.4–13.1 Å. This configuration provides a range of
momentum transfers of 0.004 Å–1 < q < 0.45 Å–1, where q = 4π sin(θ)/λ, 2θ is the scattering
angle, and λ is the wavelength. Samples were loaded into 1 mm
path length cylindrical quartz cuvettes from Hellma (Plainview, NY).
The original standard sample environment of the instrument50 (link) was used to control the temperature to within
±1 °C by means of a water bath. Data reduction followed
standard procedures.51 (link) The data reduction
included the subtraction of the appropriate solvent background.
were made using the EQ-SANS instrument at the Spallation Neutron Source
of Oak Ridge National Laboratory.49 (link) A single
configuration was used for all measurements. A sample-to-detector
distance of 4 m was employed with a minimum wavelength setting of
2.5 Å. The choppers ran at 30 Hz in the “frame-skipping”
mode. As a result, the wavelength bands were 2.5–6.1 Å
and 9.4–13.1 Å. This configuration provides a range of
momentum transfers of 0.004 Å–1 < q < 0.45 Å–1, where q = 4π sin(θ)/λ, 2θ is the scattering
angle, and λ is the wavelength. Samples were loaded into 1 mm
path length cylindrical quartz cuvettes from Hellma (Plainview, NY).
The original standard sample environment of the instrument50 (link) was used to control the temperature to within
±1 °C by means of a water bath. Data reduction followed
standard procedures.51 (link) The data reduction
included the subtraction of the appropriate solvent background.
3
Multi-angle Dynamic Light Scattering
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For multi-angle DLS, cylindrical quartz cuvettes (Hellma, Mu ¨hlheim, Germany) were cleaned by dust-free distilled acetone and transferred to a dust free flow box. Solutions were filtered into the cuvettes through Pall GHP filters, 0.45 mm pore size. DLS measurements were performed by the following instrument at 20 1C. The apparatus consists of a Uniphase He/Ne Laser (22.5 mW output power at l = 632.8 nm) and an ALV/CGS-8F SLS/DLS 5022F goniometer with eight simultaneously working ALV 7004 correlators and eight ALV/High QEAPD avalanche photodiode detectors. The correlation functions of the particles were fitted using a sum of two exponentials. The z-average diffusion coefficient D z was calculated by extrapolating D app for q = 0. By formal application of Stokes law, the inverse z-average hydrodynamic radius is
4
Nanoparticle Size Distribution Analysis
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Size distributions of the nanoparticle dispersions and nanoparticle-protein corona complexes were determined on an ALV spectrometer (ALV, Langen, Germany) consisting of a goniometer and an ALV-5004 multiple-tau full-digital correlator (320 channels) allowing measurements over an angular range from 30 to 150°. As light source a He-Ne laser (JDS Uniphase, Milpitas, USA)
working at an output power of 25 mW and a wavelength of 632.8 nm was utilized. For light scattering experiments, pure nanoparticle samples were filtered through 0.45 m Millex LCR filters (Millipore) into cylindrical quartz cuvettes with an outer diameter of 20 mm (Hellma, Müllheim, Germany). The cuvettes were cleaned by dust-free distilled acetone in a special acetone fountain prior to use in experiments. For the size determination of the nanoparticles, they were diluted in MilliQ water to a concentration of 0.01 mg mL -1 . The nanoparticles were analyzed according to the CONTIN algorithm [39, 40] and the obtained diffusion coefficients for each scattering vector q were extrapolated to q 0. The extrapolated Dz was converted into the Rh applying Stokes law (Rh = kBT/6D; Rh is the hydrodynamic radius, while kB, T, and D represent the Boltzmann constant, temperature, viscosity and diffusion coefficient, respectively).
working at an output power of 25 mW and a wavelength of 632.8 nm was utilized. For light scattering experiments, pure nanoparticle samples were filtered through 0.45 m Millex LCR filters (Millipore) into cylindrical quartz cuvettes with an outer diameter of 20 mm (Hellma, Müllheim, Germany). The cuvettes were cleaned by dust-free distilled acetone in a special acetone fountain prior to use in experiments. For the size determination of the nanoparticles, they were diluted in MilliQ water to a concentration of 0.01 mg mL -1 . The nanoparticles were analyzed according to the CONTIN algorithm [39, 40] and the obtained diffusion coefficients for each scattering vector q were extrapolated to q 0. The extrapolated Dz was converted into the Rh applying Stokes law (Rh = kBT/6D; Rh is the hydrodynamic radius, while kB, T, and D represent the Boltzmann constant, temperature, viscosity and diffusion coefficient, respectively).
5
Circular Dichroism Analysis of Peptides and Proteins
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Peptides and purified protein constructs were characterized in circular dichroism (CD) spectroscopy. For that, peptides were directly dissolved in degassed ultrapure Milli-Q water (Millipore) or degassed and filtered (0.22-µm filter) CD buffer (10 mM KH2PO4/K2HPO4, pH 8.0 at 20 °C) and subsequently diluted to 0.10 mg mL−1. Original buffer of protein samples was exchanged for the CD buffer on a desalting PD MiniTrap G-25 column (GE Healthcare Life Sciences). Protein and fos-choline-16 concentrations were determined by using a Direct Detect infrared spectrometer (EMD Millipore) and the samples diluted to final protein concentration 0.10–0.20 mg mL−1. Fos-choline-16 was added to each blank buffer solution to match detergent concentration in the final protein samples. CD spectra were recorded at room temperature on a J-715 spectropolarimeter (JASCO) using a 1-mm-path-length cylindrical quartz cuvette (Hellma). Each spectrum represents an average of 10 continuous scans (100 nm min−1) with response time 0.25 s and bandwidth 1.0 nm. CD spectra of the peptides were analysed using the K2D2 web server49 (link) (Supplementary Fig. S3b,c ). Secondary structure content of the protein constructs was calculated in programs CDSSTR50 , CONTIN51 (link) and SELCON352 (link),53 (link) from CDPro software package54 (link) using the reference protein set SMP50 (Supplementary Fig. S10 and S11 ).
6
Circular Dichroism of ETR1 Tryptophan Mutants
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CD measurements of ETR1 tryptophan mutants were performed using a Jasco-715 spectropolarimeter (Jasco GmbH, Gross-Umstadt, Germany) and a cylindrical quartz cuvette (Hellma GmbH & Co. KG, Muellheim) with a path length of 1 mm and a volume of 200 μl. All measurements were performed at room temperature in buffer C at a protein concentration of 0.1–0.3 mg/ml. Spectra were recorded from 260–195 nm with a step resolution of 1 nm and a bandwidth of 2 nm. The scan speed was set to 50 nm/min, and 10 scans were accumulated. Secondary structure content of purified proteins was calculated from the spectra by Selcon3 and CONTINLL.
7
Circular Dichroism Analysis of Tomato Receptors
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CD measurements were performed in a Jasco J715 spectropolarimeter (Jasco GmbH, Gross-Umstadt, Germany). For the far UV spectra a cylindrical quartz cuvette from Hellma Analytics (Muellheim, Germany) with 1-mm-path-length was used. Purified tomato receptors LeETR4 and NR were dissolved to a final concentration of 0.2 mg ml-1 in 10 mM potassium phosphate pH 8.0 and 0.0075% (w/v) FosCholine-16. Protein and FosCholine-16 concentrations were determined by a Direct Detect Infrared Spectrometer (Merck Chemicals GmbH, Darmstadt, Germany) (Strug et al., 2014 (link)). For detailed information on protein preparation see Kessenbrock and Groth (2017) (link). Measurements were run at ambient temperature. Each protein sample was recorded in the range of 260–185 nm. The CD spectra were obtained by averaging ten individual spectra using a bandwidth of 1 nm at 50 nm min-1. Secondary structure content of purified proteins were calculated from the spectra by CDSSTR and CONTINLL (Provencher and Gloeckner, 1981 (link); Johnson, 1999 (link)).
8
Circular Dichroism Analysis of Aip5 Protein
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Eighty µl of 0.5 mg/ml purified Aip5 proteins were prepared in a buffer (20 mM Tris pH 7.6, 50 mM NaCl) and then loaded in the water-jacketed, 1 mm path length cylindrical quartz cuvette (Hellma). The CD spectra were collected using a Jasco J-710 spectropolarimeter at 0.5 nm resolution and a scan rate of 200 nm/min at room temperature. Reported spectra were averages of three scans and smoothed. Reported molar ellipticities were calculated by subtracting the background spectrum in the Chriascan CD Spectrometer.
9
Circular Dichroism Spectroscopy of Bnr1 Proteins
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Three hundred microliters of 0.15 mg/ml purified Bnr1-C and 0.075 mg/ml purified Bnr1-LC proteins were prepared in a buffer (50 mM phosphate-buffered saline, pH 7.4) and then loaded in the water-jacketed, 1-mm path length cylindrical quartz cuvette (Hellma). The CD spectra were collected using a Jasco J-710 spectropolarimeter at 1 nm resolution and a scan rate of 200 nm /min at room temperature. Reported molar ellipticities were calculated by subtracting the background spectrum in the Chriascan CD Spectrometer. The CD spectrum was then subjected to DichroWeb (http://dichroweb.cryst
.bbk.ac.uk/html/home.shtml ) with K2D program for secondary structure analysis (Whitmore and Wallace, 2004 (link), 2008 (link)).
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