The 1H NMR spectra of CP-1, CP-3, CP-1-Fe and CP-3-Fe (20.00 mg) were recorded by a Bruker Advance III 500 MHz instrument (Bruker AVIII500, Swit.). CP-1, CP-3, CP-1-Fe and CP-3-Fe (20 mg) were dissolved in D2O, freeze-dried three times and then placed in a NMR tube at 400 MHz at room temperature.
Aviii 500
Manufactured by Bruker
Sourced in Switzerland, Germany, United States
The AVIII 500 is a high-performance nuclear magnetic resonance (NMR) spectrometer designed for advanced analytical applications. It features a 500 MHz superconducting magnet and a range of hardware and software components to enable precise measurements and analysis of chemical and biological samples.
Automatically generated - may contain errors
Lab products found in correlation
Aviii400, by Bruker (4 mentions)
Drx 500, by Bruker (3 mentions)
Av 400, by Bruker (3 mentions)
Aviii hd 400, by Bruker (2 mentions)
Dpx 300, by Bruker (2 mentions)
Dpx 400, by Bruker (2 mentions)
Silica gel geduran si 60, by Merck Group (2 mentions)
Silica gel 60 f254, by Merck Group (2 mentions)
Aviii 800, by Bruker (2 mentions)
Aviii 600, by Bruker (2 mentions)
Anhydrous benzene, by Merck Group (1 mentions)
Alpha 2 spectrometer, by Bruker (1 mentions)
Amicon ultra centrifugal filter, by Merck Group (1 mentions)
Topspin 2, by Bruker (1 mentions)
Emx epr spectrometer, by Bruker (1 mentions)
Microtof spectrometer, by Bruker (1 mentions)
25 spectrometer, by PerkinElmer (1 mentions)
Ultraflex 3 maldi tof spectrometer, by Bruker (1 mentions)
Lc msd tof, by Agilent Technologies (1 mentions)
Aviii 900, by Bruker (1 mentions)
25 protocols using aviii 500
1
Comparative NMR Analysis of Metallocomplex Compounds
2
Preparation and Characterization of Organometallic Compounds
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THF, Et2O, toluene and hexane were passed through columns containing molecular sieves, then stored over molecular sieves (THF) or over a potassium mirror (Et2O, hexane, toluene) and thoroughly degassed prior to use. Anhydrous benzene was purchased from Sigma Aldrich, stored over a potassium mirror and thoroughly degassed prior to use. For NMR spectroscopy, C6D6 and C4D8O were dried by refluxing over K, CDCl3 was dried by refluxing over CaH2; NMR solvents were then vacuum transferred and degassed by three freeze-pump-thaw cycles before use. NMR spectra were recorded on either a Bruker AVIII HD 400 or Bruker AVIII 500 spectrometer operating at 400.07/500.13 (1H), 100.60/125.78 (13C{1H}), 376.46 (19F{1H}) MHz. NMR spectra were recorded at 298 K unless otherwise stated and were referenced to residual solvent signals in the case of 1H and 13C{1H} experiments. FTIR spectra were recorded on a Bruker Alpha II spectrometer with a Platinum-ATR module. Elemental microanalyses were carried out by Elemental Microanalysis Ltd. Lawson’s reagent, 6-trifluoromethyl-2-pyridone, 2-mercaptopyridine, potassium hydroxide, bromoform, isopropylmagnesium chloride, methylmagnesium bromide, and methylmagnesium iodide were used as received. HTptm [25 (link)], 2-mercapto-6-trifluoromethylpyridine [32 (link)], and benzyl potassium [33 (link)] were prepared according to literature procedures.
3
RNA Secondary Structure Characterization
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RNA was prepared to a concentration of 0.03-0.5 mM in 10 mM lithium cacodylate, 1 mM KCl or LiCl, pH 5.8 using 3’000 NMWL Amicon Ultra Centrifugal Filters (Merck Millipore Ltd., IRL). After heating to 95°C for 5 min KCl (100 or 200 mM), NaCl (100 mM) or MgCl2 (2 mM) was added directly to the warm solution containing the oligonucleotides. The samples were then progressively cooled down to room temperature for 60 min before to be stored on ice. One-dimensional watergate 1H NMR spectra 2D 1H 15N HSQC and 2D 1H-1H noesy spectra were recorded at 288 K on Bruker AVIII-500, 600 and 900 MHz spectrometers equipped with a cryoprobe. Topspin 2.1 (Bruker) was used for data processing. The secondary structure of the hairpin RNA was illustrated with the RNA visualization toolforna (Kerpedjiev et al., 2015 (link)).
4
NMR Relaxation Time Measurements
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The 13C relaxation times
(T1) were measured with a standard inversion
recovery pulse sequence on a Bruker AVIII HD 400 instrument operating
at 400.13 MHz (1H) and 100.61 MHz (13C) equipped
with a 5 mm DUL probe fort the direct observation of the 13C nucleus (Figures S9–S12 ). 1H and 31P NMR and bi-dimensional experiments were
performed on a Bruker AVIII 500 instrument operating at 500.13 MHz
(1H) and 202.46 MHz (31P), equipped with a 5
mm z-gradient BBI probe (Figure 6 ).
(T1) were measured with a standard inversion
recovery pulse sequence on a Bruker AVIII HD 400 instrument operating
at 400.13 MHz (1H) and 100.61 MHz (13C) equipped
with a 5 mm DUL probe fort the direct observation of the 13C nucleus (
performed on a Bruker AVIII 500 instrument operating at 500.13 MHz
(1H) and 202.46 MHz (31P), equipped with a 5
mm z-gradient BBI probe (
5
Fullerene Derivatives Synthesis and Characterization
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C60 (99.5%) and C70 (95%) were purchased from SES Research and MER corporation respectively. CH2Cl2 was freshly distilled over CaH2 before use. All other reagents and solvents were purchased from Aldrich and used without further purification. Compounds 1 –3 and 7 –10 were synthesised according to previously reported procedure [20 (link)]. Infra-red spectra were measured as KBr discs using a Nicolet Avatar 380 FTIR spectrometer over the range 400–4000 cm−1. 1H and 13C NMR spectra were obtained using Bruker DPX 300, Bruker DPX 400, Bruker AV(III) 400 or Bruker AV(III) 500 spectrometers. Mass spectrometry was carried out using a Bruker microTOF spectrometer and a Bruker ultraFlexIII MALDI–TOF spectrometer using trans-2-[3-(4-tert-butylphenyl)-2-methyl-2-propenylidene]malononitrile (DCTB) as supporting matrix. UV–vis spectra were measured using a Lambda 25 Perkin Elmer Spectrometer. EPR spectra were obtained on a Bruker EMX EPR spectrometer.
6
Detailed Spectroscopic Characterization of Organic Compounds
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All reagents obtained from commercial sources were used without purification, unless otherwise mentioned. Column chromatography was carried out by Silica Gel Geduran® Si 60 (0.040–0.063 mm, E. Merck). TLC was performed on pre-coated glass plates of Silica Gel 60 F254 (0.25 mm, E. Merck); detection was executed by spraying with a solution of Ce(SO4)2 (NH4)2MoO4, and H2SO4 in water and subsequently heating on a hot plate. UV light for TLC analysis was UVGL-25 compact UV lamp (4 watt/254 nm). Melting points were determined with a MP-2D melting apparatus. 1H NMR, 13C NMR, and DEPT spectra were recorded by Bruker DRX500 and AVIII 500. Chemical shifts are in ppm from Me4Si, generated from the DMSO-d6 and CDCl3 lock signal at δ 2.50, 7.24 and 40.00, 77.16 ppm for 1H and 13C NMR, respectively. Multiplicities are reports by using the following abbreviations: s = singlet, d = doublet, t = triplet, q = quartet, p = pentet, s = sextet, m = multiplet, br = broad, dd = doublet of doublets, dt = doublet of triplets, td = triplet of doublets; J = coupling constant values in Hertz. High resolution mass spectrometry (HR-MS) was performed on a Waters Premier XE instrument with ESI source. Structural assignments were made with additional information from selective 1D-TOCSY, 2D-HSQC, 2D-HMBC and X-ray experiments.
7
Synthesis and Characterization of Rhodium Complexes
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Manipulations were performed under an inert atmosphere, using Schlenk and glove box
techniques unless otherwise stated. Glassware was oven dried and flamed under vacuum prior
to use. Anhydrous solvents (<0.005% H2O) were purchased from ACROS or
Aldrich and used as supplied: Et2O, CHCl3, pentane,
CH2Cl2, THF and toluene. CD2Cl2 was dried
over molecular sieves (4 Å) and stored under an atmosphere of argon. Na[BArF4],27 [Rh(CO)2Cl]2,28 and1 ·2HBr19c were synthesised using literature procedures. All other reagents are commercial
products and were used as received. NMR spectra were recorded on Bruker HD-300, DPX-400,
AV-400, DRX-500 and AVIII-500 HD spectrometers at 298 K unless otherwise stated. Chemical
shirts are quoted in ppm and coupling constants in Hz. ESI-MS were recorded on a Bruker
MaXis mass spectrometer. Microanalyses were performed at the London Metropolitan
University by Stephen Boyer.
techniques unless otherwise stated. Glassware was oven dried and flamed under vacuum prior
to use. Anhydrous solvents (<0.005% H2O) were purchased from ACROS or
Aldrich and used as supplied: Et2O, CHCl3, pentane,
CH2Cl2, THF and toluene. CD2Cl2 was dried
over molecular sieves (4 Å) and stored under an atmosphere of argon. Na[BArF4],27 [Rh(CO)2Cl]2,28 and
products and were used as received. NMR spectra were recorded on Bruker HD-300, DPX-400,
AV-400, DRX-500 and AVIII-500 HD spectrometers at 298 K unless otherwise stated. Chemical
shirts are quoted in ppm and coupling constants in Hz. ESI-MS were recorded on a Bruker
MaXis mass spectrometer. Microanalyses were performed at the London Metropolitan
University by Stephen Boyer.
8
Spectroscopic Characterization of Organic Compounds
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All compounds were fully characterized by spectroscopic data. The NMR spectra were recorded on Bruker AVIII-400 (1H: 400 MHz, 13C: 100 MHz) or Bruker AVIII-500 (1H: 500 MHz, 13C: 125 MHz) and chemical shifts (δ) are expressed in ppm, and J values are given in Hz, CDCl3 was used as solvent. IR spectra were recorded on a FT-IR Thermo Nicolet Avatar 360 using a KBr pellet. The reactions were monitored by thin-layer chromatography (TLC) using silica gel GF254. The melting points were determined on XT-4A melting point apparatus and are uncorrected. HRMS were performed on a Agilent LC/Msd TOF and monoisotopic mass instrument.
9
NMR Spectroscopy of Compound Mixtures
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For NMR measurements, PPI and PSPF powder were completely dissolved in 0.5 mL of dimethyl-d6 sulfoxide (D-DMSO) and transferred into an NMR tube. The 1H spectra experiments were recorded at room temperature at 500 MHz on a spectrometer (AVIII500, Bruker, Fällanden, Switzerland).
10
NMR Characterization of Edc3 Protein Interactions
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All solution-state NMR samples were in buffer 4 and contained 5% D2O. NMR spectra were recorded at 298 K on Bruker AVIII-500 and AVIII-800 spectrometers equipped with room temperature and cryo probe heads, respectively. NMR titration experiments were carried out with 0.05–0.1 mm 15N- and ILVM methyl-labeled protein (Edc3 YjeF) and a four- to sixfold excess of unlabeled protein (Edc3 IDR). NMR spectra were processed using the NMRPipe/NMRDraw software suite45 (link). Figures displaying NMR spectra and protein structures were produced using NMRview (onemoonscientific.com) and Pymol (pymol.org), respectively. Solution-state NMR parameters are given in an overview in Supplementary Table 5 .
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