Optical rotations were measured on a JASCO P-2000 polarimeter, UV/Vis data were obtained using a Beckman DU800 spectrophotometer, and IR spectra were recorded on a Nicolet 100 FT-IR spectrometer. NMR data were obtained on a JEOL ECZ 500 NMR spectrometer equipped with a 3 mm inverse probe (H3X), the 1,1-ADEQUATE experiment was performed on a Bruker AVANCE III 600 MHz NMR with a 1.7 mm dual tune TCI cryoprobe. NMR data were recorded in either DMSO-d6 or methanol-d4 and adjusted to the residual solvent peak (DMSO-d6 δH 2.50, δC 39.52; methanol-d4 δH 3.31, δC 49.00). For HPLC-MS analysis, a Thermo Finnigan Surveyor HPLC system with a Phenomenex Kinetex 5 μm C18 100 × 4.6 mm column coupled to a Thermo-Finnigan LCQ Advantage Max Mass Spectrometer was used. Samples were analyzed using a linear gradient with (A) H2O + 0.1% FA to (B) CH3CN + 0.1% FA at a flow rate of 0.6 ml/min and UV detection at 220 nm, 254 nm and 280 nm. For HR-ESI-MS analysis, an Agilent 6530 Accurate Mass QTOF mass spectrometer was used in the positive ion mode. Semi-preparative HPLC was performed on a Thermo Fisher Scientific HPLC system with a Thermo Dionex UltiMate 3000 pump, RS autosampler, RS diode array detector, and automated fraction collector. All solvents were HPLC grade except for H2O, which was purified by a Millipore Milli-Q system before use.
Avance 3 600 mhz nmr
Manufactured by Bruker
Sourced in Germany, United States
The Avance III 600 MHz NMR is a high-performance nuclear magnetic resonance spectrometer designed for advanced analytical applications. It features a 600 MHz superconducting magnet and a range of state-of-the-art hardware and software components to enable precise and accurate data acquisition and analysis.
Automatically generated - may contain errors
Lab products found in correlation
Milli q system, by Merck Group (2 mentions)
Hplc system, by Thermo Fisher Scientific (2 mentions)
Surveyor hplc system, by Phenomenex (1 mentions)
Lcq advantage max mass spectrometer, by Thermo Fisher Scientific (1 mentions)
Accurate mass qtof mass spectrometer, by Agilent Technologies (1 mentions)
Ecz 500 nmr spectrometer, by JEOL (1 mentions)
Ultimate 3000 pump, by Thermo Fisher Scientific (1 mentions)
Dimethylformamide, by Merck Group (1 mentions)
Bbfo cryoprobe, by Bruker (1 mentions)
Topspin 3, by Bruker (1 mentions)
P 2000 polarimeter, by Jasco (1 mentions)
Deuterated nmr solvents, by Cambridge Isotopes (1 mentions)
Rs diode array detector, by Thermo Fisher Scientific (1 mentions)
Agilent 6530 accurate mass q tof mass spectrometer, by Agilent Technologies (1 mentions)
Beckman du800 spectrophotometer, by Beckman Coulter (1 mentions)
Rs autosampler, by Thermo Fisher Scientific (1 mentions)
Avance 3 700 mhz spectrometer, by Bruker (1 mentions)
Zorbax eclipse xdb c18, by Agilent Technologies (1 mentions)
14 protocols using avance 3 600 mhz nmr
1
Analytical Techniques for Chemical Characterization
2
Synthesis and Characterization of Organic Compounds
3
NMR Spectroscopic Characterization of Compounds
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NMR spectra (1H, 13C NMR, 1H-1H COSY, HMBC and HMQC) were acquired in CD3OD or DMSO-d6 at 25 °C using a Bruker Avance III 600 MHz NMR spectrometer (Bruker BioSpin, Rheinstetten, Germany) and TMS as an internal standard.
4
Monitoring P36 Interaction with P. aeruginosa
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P. aeruginosa cultures were grown overnight and
used to
perform the experiment. The cell suspensions were centrifuged at 6000
rpm for 5 min. Cell pellets were washed three times with 10 mM phosphate
buffer at pH 6.5 and later resuspended in the same buffer to obtain
a cell suspension containing 106 CFU/mL. One-dimensional
(1D) proton NMR spectra of 1 mM solution ofP36 in a
mixture of 90% of 10 mM phosphate buffer (pH 6.5) and 10% D2O was recorded on a Bruker Avance III 600 MHz NMR spectrometer. In
another experiment, 500 μg of solid peptideP36 was added to a 500 μL solution of the cells (106 CFU/mL), and the mixture was thoroughly vortexed to achieve a final
peptide concentration of 1 mM. A series of 1D 1H NMR spectra
were recorded at different time points after addition ofP36 to the P. aeruginosa cells. The temperature for
the experiment was adjusted as per the standard growing temperature
of P. aeruginosa at 310 K.
used to
perform the experiment. The cell suspensions were centrifuged at 6000
rpm for 5 min. Cell pellets were washed three times with 10 mM phosphate
buffer at pH 6.5 and later resuspended in the same buffer to obtain
a cell suspension containing 106 CFU/mL. One-dimensional
(1D) proton NMR spectra of 1 mM solution of
mixture of 90% of 10 mM phosphate buffer (pH 6.5) and 10% D2O was recorded on a Bruker Avance III 600 MHz NMR spectrometer. In
another experiment, 500 μg of solid peptide
peptide concentration of 1 mM. A series of 1D 1H NMR spectra
were recorded at different time points after addition of
the experiment was adjusted as per the standard growing temperature
of P. aeruginosa at 310 K.
5
NMR Profiling of Liver and Cecal Metabolites
6
NMR Spectroscopic Analysis of Chemical Compounds
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All NMR measurements were performed at 298 K on a Bruker Avance III 600 MHz NMR spectrometer equipped with a BBFO cryoprobe (Bruker Bio Spin, Rheinstetten, Germany). One-dimensional (1D) 1H spectra were acquired using the pulse sequence NOESYGPPR1D [RD-G1- 90°-t-90°-τm-G2-90°-ACQ] with the following acquisition parameters: relaxation delay (RD), 4 s; short delay (t), 4 μs; mixing time (τm), 10 ms; spectral width, 20 ppm; acquisition time, 1.93 s; and 128 transients. The methyl groups of the TSP molecule were set at 0 ppm for chemical shift calibration. The two-dimensional (2D) 1H–13C heteronuclear single quantum coherence (HSQC) spectrum was recorded with a spectral width of 10 ppm in the 1H dimension and 110 ppm in the 13C dimension, a data matrix of 1024 × 256 points, and a relaxation delay of 1.5 s. The 2D total correlation spectroscopy (TOCSY) spectrum was recorded with a spectral width of 10 ppm in both 1H dimensions, a data matrix of 2048 × 256 points, and a relaxation delay of 1.5 s.
7
NMR Characterization of Reaction Mixtures
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The
reaction mixtures
were prepared in the fumehood, mixed in a tube, and allowed to equilibrate.
After 15 min the mixtures were relatively stable, and the conventional
NMR measurements were performed typically after a reaction time of
around 2 h. After the desired reaction time, a sample was taken and
put into a 5 mm (500 μL) NMR tube and subsequently measured
with a commercially available probe in a Bruker Avance III 600 MHz
NMR spectrometer operated with Bruker TopSpin 3.0 software. For each
sample, a 1H spectrum, a 13C spectrum, a heteronuclear
single quantum coherence (HSQC)61 (link) spectrum,
and a heteronuclear multiple-bond correlation (HMBC)62 (link) spectrum was taken.
reaction mixtures
were prepared in the fumehood, mixed in a tube, and allowed to equilibrate.
After 15 min the mixtures were relatively stable, and the conventional
NMR measurements were performed typically after a reaction time of
around 2 h. After the desired reaction time, a sample was taken and
put into a 5 mm (500 μL) NMR tube and subsequently measured
with a commercially available probe in a Bruker Avance III 600 MHz
NMR spectrometer operated with Bruker TopSpin 3.0 software. For each
sample, a 1H spectrum, a 13C spectrum, a heteronuclear
single quantum coherence (HSQC)61 (link) spectrum,
and a heteronuclear multiple-bond correlation (HMBC)62 (link) spectrum was taken.
8
NMR Characterization of Deuterium-Exchanged Protein
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The FVPT1 was dissolved with D2O and lyophilized in a vacuum freeze dryer to facilitate deuterium exchange. The deuterium-exchanged FVPT1 (40 mg) was dissolved in 0.5 mL of 99.96% D2O for NMR. 1H,13C, Nuclear Overhauser Effect Spectroscopy (NOESY), heteronuclear multiple quantum coherence (HMQC) and 1H-detected heteronuclear multiple-bond correlation (HMBC) NMR spectra were recorded at 27 °C on a Bruker Avance III 600 MHz NMR spectrometer (Bruker Corporation (Billerica, MA, USA)). 1H chemical shifts were referenced to residual HDO, with δ 4.78 ppm (27 °C) as the internal standard. 13C chemical shifts were determined in relation to DSS (δ 0.00 ppm) calibrated externally. The 1H-1H-correlated spectroscopy (COSY) and HMQC were used to assign signals. HMBC and NOESY were used to assign inter-residue linkages and sequences.
9
Spectroscopic Characterization of Compounds
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Optical rotations were measured on a JASCO P-2000 polarimeter (JASCO Corporation, Tokyo, Japan), UV/Vis data were obtained using a Beckman DU800 spectrophotometer (Beckman Coulter, Brea, CA, USA), and IR spectra were recorded on a Nicolet 100 FT-IR spectrometer (Nicolet, Madison, WI, USA). NMR data were obtained on a Bruker AVANCE III 600 MHz NMR with a 1.7 mm dual tune TCI cryoprobe (Bruker, Billerica, MA, USA) and the 1D TOCSY experiments were performed on a JEOL ECZ 500 NMR spectrometer equipped with a 3 mm inverse probe (H3X) (JEOL Ltd., Tokyo, Japan). Data were recorded in either pyridine-d5 or methanol-d4 and adjusted to the residual solvent peak (pyridine-d5 δH 7.22, δC 123.87; methanol-d4 δH 3.31, δC 49.00). Deuterated NMR solvents were purchased from Cambridge Isotope Laboratories (Tewksbury, MA, USA). For high resolution electrospray mass spectrometric analysis (HR–ESI–MS), an Agilent 6530 Accurate Mass QTOF mass spectrometer was used in the positive ion mode (Agilent, Santa Clara, CA, USA). Semi-preparative HPLC was performed on a Thermo Fisher Scientific HPLC system with a Thermo Dionex UltiMate 3000 pump, RS autosampler, RS diode array detector, and automated fraction collector (Thermo Fisher Scientific, Waltham, MA, USA). All solvents were HPLC grade except for water, which was purified by a Millipore Milli-Q system before use.
10
NMR Characterization of Modified DNA
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