HPLC separations were accomplished using a Varian Prostar instrument. Laser desorption/ionization time-of-flight (LDI-TOF) mass spectrometry was conducted on a Bruker Microflex LRF mass spectrometer. Vis-NIR spectra were obtained with a Cary 5000 UV-Vis-NIR spectrophotometer in toluene. Cyclic voltammograms (CV) and square wave voltammograms (SWV) were measured in o-dichlorobenzene with 0.05 M n-Bu4NPF6 as the supporting electrolyte using a CH Instrument Potentiostat. A 1 mm diameter glassy carbon disk was used as the working electrode, with a platinum wire and silver wire as the counter reference electrodes, respectively. All potentials were reported relative to the Fc/Fc+ couple.
Prostar instrument
Manufactured by Agilent Technologies
The Prostar instrument is a versatile analytical tool designed for a range of laboratory applications. It functions as a modular high-performance liquid chromatography (HPLC) system, capable of performing various separation and detection techniques. The Prostar instrument allows for the efficient and reliable analysis of complex samples.
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3 protocols using prostar instrument
1
Analytical Characterization of Organic Compounds
2
Synthesis and Characterization of Poly(Lactide)
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All reactions that involved
compounds sensitive to air and/or moisture were carried out under
a dry nitrogen atmosphere using freshly dried solvents and standard
Schlenk line and glovebox techniques. All chemicals were purchased
from commercial sources. Toluene, hexanes, and THF were distilled
under nitrogen from Na/benzophenone. CDCl3 was dried over
CaH2, distilled, and degassed prior to use. rac-LA was recrystallized from dry toluene, sublimed under vacuum, and
stored under a dry nitrogen atmosphere.
NMR spectra were recorded
on a Bruker AVANCE-500 NMR spectrometer (1H, and 13C) and referenced to the residual solvent peak. J values are given in Hz. Gel permeation chromatography (GPC) analysis
was performed on a Varian Prostar instrument, using a PLgel 5 μm
Mixed-D column, a Prostar 355 RI detector, and THF as eluent at a
flow rate of 1 mL/min (20 °C). Polystyrene standards were used
for calibration. Matrix-assisted laser desorption/ionization time-of-flight
mass spectrometry (MALDI-TOF MS) spectra were obtained on Applied
Biosystems/MD SCIEX 4800 equipment using α-cyano-4-hydroxycinnamic
acid as a matrix and 5 mM sodium acetate as an ionization agent. The
HR-MS was performed using high-resolution time-of-flight G1969A instrumentation
(Agilent). The optical rotation was measured on a Jasco P-2000 polarimeter
with a 589 nm light source at 23 °C.
compounds sensitive to air and/or moisture were carried out under
a dry nitrogen atmosphere using freshly dried solvents and standard
Schlenk line and glovebox techniques. All chemicals were purchased
from commercial sources. Toluene, hexanes, and THF were distilled
under nitrogen from Na/benzophenone. CDCl3 was dried over
CaH2, distilled, and degassed prior to use. rac-LA was recrystallized from dry toluene, sublimed under vacuum, and
stored under a dry nitrogen atmosphere.
NMR spectra were recorded
on a Bruker AVANCE-500 NMR spectrometer (1H, and 13C) and referenced to the residual solvent peak. J values are given in Hz. Gel permeation chromatography (GPC) analysis
was performed on a Varian Prostar instrument, using a PLgel 5 μm
Mixed-D column, a Prostar 355 RI detector, and THF as eluent at a
flow rate of 1 mL/min (20 °C). Polystyrene standards were used
for calibration. Matrix-assisted laser desorption/ionization time-of-flight
mass spectrometry (MALDI-TOF MS) spectra were obtained on Applied
Biosystems/MD SCIEX 4800 equipment using α-cyano-4-hydroxycinnamic
acid as a matrix and 5 mM sodium acetate as an ionization agent. The
HR-MS was performed using high-resolution time-of-flight G1969A instrumentation
(Agilent). The optical rotation was measured on a Jasco P-2000 polarimeter
with a 589 nm light source at 23 °C.
3
Synthesis and Purification of Fluorescent H4 Peptide
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In all the stopped flow fluorescence assays, H4FL peptides (the N-terminal 20 amino acids of histone H4, with Leu-10 replaced by fluorescein-labeled Lys-10) were used as probes.33 (link) H4FL was synthesized using the Fmoc-based solid phase peptide synthesis (SPPS) protocol on a PS3 peptide synthesizer (Protein Technology, Arizona, USA) as described previously.33 (link) Each amino acid was coupled to the solid phase with HCTU [O-(1H-6-chlorobenzotriazole-1-yl)-1,1,3,3- tetramethyluronium hexafluorophosphate] (Novabiochem, Darmstadt, Germany), using 4 equivalents of amino acid. The Fmoc group was deprotected with 20% v/v piperidine/DMF, and the N-terminal amino acid was acetylated with acetic anhydride. The peptide was cleaved from the Wang resin by a cleavage solution consisting of 95% trifluoroacetic acid (TFA), 2.5% H2O, and 2.5% triisopropylsilane. It was then precipitated in cold ether and pelleted by centrifugation. Crude peptides were collected and purified using a Varian Prostar instrument equipped with a C18 reversed-phase high-performance liquid chromatography (RP-HPLC) column, where 0.05% TFA in water and 0.05% TFA in acetonitrile were the two mobile phases used for gradient purification. The identity of peptides was confirmed by MALDI-MS. The concentrations of the peptides were calibrated according to the absorption of fluorescein at 492 nm.
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