Prodigy bbo cryoprobe

Manufactured by Bruker

Sourced in United States, Germany, Switzerland

The Prodigy BBO cryoprobe is a specialized laboratory equipment designed for high-resolution nuclear magnetic resonance (NMR) spectroscopy. It features a broadband observe (BBO) coil configuration and cryogenic cooling technology to enhance the signal-to-noise ratio and improve the overall performance of NMR experiments.

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Lab products found in correlation

Avance 2 600 mhz spectrometer, by Bruker (1 mentions) Nmr suite profiling software, by Chenomx (1 mentions) Tci cryoprobe, by Bruker (1 mentions) Avance 3, by Bruker (1 mentions) Avance 3 hd 500 nmr, by Bruker (1 mentions) Avance 3 hd spectrometer, by Bruker (1 mentions) Bbfo probe, by Bruker (1 mentions) Avance 3 hd, by Bruker (1 mentions) Topspin 3.5pl7, by Bruker (1 mentions)

Close spelling variants of this product

CryoProbe (153 citations) Prodigy cryoprobe (24 citations)

8 protocols using prodigy bbo cryoprobe

NMR Profiling of Cellular Metabolites

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The experiments were conducted using 200 μL cell extracts samples in 103.5 mm x 3 mm NMR tubes (Bruker Analytik, Rheinstetten, Germany) and 550 μL media samples in 103.5 mm x 5 mm NMR tubes. The data was acquired on a Bruker Avance II 600 MHz spectrometer with Prodigy BBO cryoprobe as previously described (Maki et al., 2020 (link)). Metabolites were assigned based on 1D ¹H and 2D NMR experiments by comparing the chemical shifts with reference spectra found in databases, such as the Human Metabolome Database (HMDB) (Wishart et al., 2007 (link)), the Madison metabolomics consortium database (MMCD) (Cui et al., 2008 ), the biological magnetic resonance data bank (BMRB) (Ulrich et al., 2008 (link)), and Chenomx® NMR Suite profiling software (Chenomx Inc. version 8.1).
The quantification of metabolites was performed on Chenomx software based on the Trimethylsilylpropanoic acid (TMSP) internal reference in the NMR spectrum. The cellular metabolite concentrations were normalized to total protein extracted from each sample to normalize for the differences in number of cells per sample. Normalized metabolite concentrations (μmoles/mg total protein) were then assessed by multivariate and univariate analysis. All the multivariate analysis were performed with MetaboAnalyst 4.0 (Chong et al., 2019 (link)) and the plots were generated using Graph Pad Prism.

Wessendarp M., Watanabe-Chailland M., Liu S., Stankiewicz T., Ma Y., Kasam R.K., Shima K., Chalk C., Carey B., Rosendale L.R., Filippi M.D, & Arumugam P. (2021). Role of GM-CSF in regulating metabolism and mitochondrial functions critical to macrophage proliferation. Mitochondrion, 62, 85-101.

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NMR Spectroscopic Analysis of Organic Compounds

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The ¹H, ¹³C, ¹H-¹H COSY, ¹H-¹³C HSQC and ¹H-¹³C HMBC NMR spectra were recorded on Bruker Avance III HD spectrometers operating at a proton frequency of 600 MHz equipped with a Prodigy BBO CryoProbe or 700 MHz equipped with a TCI CryoProbe, respectively (Bruker Biospin). CD₃OD as solvent and an internal standard were used. All spectra were recorded at room temperature. Chemical shifts were expressed in parts per million (ppm, δ) relative to TMS.

Musiol-Kroll E.M., Zubeil F., Schafhauser T., Härtner T., Kulik A., McArthur J., Koryakina I., Wohlleben W., Grond S., Williams G.J., Lee S.Y, & Weber T. (2017). Polyketide bio-derivatization using the promiscuous acyltransferase KirCII. ACS synthetic biology, 6(3), 421-427.

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Determination of SBS Composition by 1H NMR

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1 H NMR spectroscopy was used to determine the wt% of PS in the neat SBS as well as the relative amount of 1,2-and 1,4-PBD using an AVANCE III HD 500 NMR (Bruker) instrument fitted with a 5 mm Prodigy BBO cryoprobe (Bruker) at 25 1C. Samples were prepared by dissolving 10-15 mg in 1 mL of deuterated chloroform, then transferred to standard NMR tubes. The SBS PS wt% was determined to be 35% and was found to be 89% 1,4-PBD (Fig. S1, ESI †).

Torres V.M., LaNasa J.A., Vogt B.D, & Hickey R.J. (2021). Controlling nanostructure and mechanical properties in triblock copolymer/monomer blends via reaction-induced phase transitions. Soft matter, 17(6).

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NMR Titration of Aptamer-Ligand Interactions

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Solution NMR spectra were recorded on a Bruker AVANCE III HD spectrometer operating at a ¹H Larmor frequency of 500 mHz a Prodigy BBO Cryoprobe (Bruker, Billerica, MA, USA). One-dimensional excitation sculpting ¹H spectra were acquired at 298 K with a 2 second recycle delay, 45.3 μs dwell time, and a 1.49 ms acquisition period. All samples were dissolved in 20 mM sodium phosphate buffer with 100 mM NaCl and 2 mM MgCl₂. All NMR samples included 10% D₂O. Before NMR analysis, aptamers were heated to 90 °C for 5 min and cooled for 15 min at room temperature. For the titration experiments, a series of spectra were recorded upon the addition of aliquots containing molar equivalents in steps of 0.0625 : 1, up to 3 : 1 ligand : aptamer, according to the concentration of each aptamer (20 μM BMAA_159 and 14.4 μM BMAA_165). Each spectrum was the average of 2048 transients. Changes in frequency intensity at the amino proton region (7.93 ppm for BMAA_159 and 7.83 ppm for BMAA_165) were plotted against the molar fraction of the target to create binding isotherms.

Santiago-Maldonado X., Rodríguez-Martínez J.A., López L., Cunci L., Bayro M, & Nicolau E. (2024). Selection, characterization, and biosensing applications of DNA aptamers targeting cyanotoxin BMAA. RSC Advances, 14(20), 13787-13800.

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H111-SOL NMR Spectroscopy Protocol

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H111-SOL sample (5 mg) was exchanged twice with 99.9% D₂O by lyophilization and then dissolved in 0.6 mL of 99.96% D₂O and introduced into a 5 mm NMR tube for data acquisition. ¹H NMR and COSY spectra were recorded using a 500 MHz VARIAN spectrometer operating at 323 K. In addition, 1D ¹H and ¹³C, and 2D, TOCSY, NOESY, HSQC, HMBC and hybrid HSQC-TOCSY and HSQC-NOESY spectra were obtained using a Bruker Advance III 600 MHz NMR spectrometer equipped with a BBO Prodigy cryoprobe and processed using standard Bruker software (Topspin 3.2). The probe temperature was set at 333 K. 2D TOCSY experiments were performed using mixing times of 180 ms and the 1D variants using mixing times up to 200 ms. The 2D NOESY experiment and 1D variants were performed using a mixing time of 300 ms. The HSQC (with multiplicity editing) experiment was optimized for J = 145 Hz (for directly attached ¹H-¹³C correlations), and the HMBC experiment optimized for a coupling constant of 8 Hz (for long-range ¹H-¹³C correlations). HSQC-TOCSY and HSQC-NOESY NMR spectra were recorded using mixing times of 120 and 300 ms, respectively. 2D experiments were recorded using non-uniform sampling: 50% for homonuclear and 25% for heteronuclear experiments. Chemical shifts are expressed in ppm using acetone as internal reference (2.225 ppm for ¹H and 31.07 ppm for ¹³C). NMR spectra were processed using MestreNova software.

Bellich B., Jou I.A., Buriola C., Ravenscroft N., Brady J.W., Fazli M., Tolker-Nielsen T., Rizzo R, & Cescutti P. (2020). The biofilm of Burkholderia cenocepacia H111 contains an exopolysaccharide composed of L-rhamnose and l-mannose: structural characterization and molecular modelling.. Carbohydrate research, 499, 108231.

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1D 1H NMR Analysis of Chemical Compounds

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1D ¹H NMR spectra were recorded on a Bruker AVANCE III HD spectrometer equipped with a 11.75 T magnet (¹H Larmor frequency of 500 MHz) and a 5 mm BBO Prodigy CryoProbe (Bruker BioSpin) abbreviated as “500 MHz spectrometer” or a Bruker AVANCE III HD spectrometer equipped with a 7.0 T magnet (300 MHz) and a 5 mm BBFO probe abbreviated as “300 MHz spectrometer”. The frequency lock was set for 10% D₂O and 90% H₂O and, followed by phase and shim adjustments. The data was acquired using a perfect echo W5 WATERGATE solvent suppression pulse sequence (adapted PEW5) with the transmitter frequency offset (o1p) centered at water signal (4.7 ppm)^{23 (link)–25 (link)}. For product identification, 512 scans were accumulated with a relaxation delay (d1) of 5 s, size of FID (td) of 32k datapoints, and an acquisition time (aq) of 3.3 s. In addition, a presaturation sequence (zgpr) was employed for comparative studies. Data was acquired with Bruker TopSpin and processed (apodization with lb value of 0.2 Hz, zero filling, phasing) with Mnova software suite.

Preikschas P., Martín A.J., Yeo B.S, & Pérez-Ramírez J. (2023). NMR-based quantification of liquid products in CO2 electroreduction on phosphate-derived nickel catalysts. Communications Chemistry, 6, 147.

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NMR Spectroscopy of Liquid Samples

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NMR spectra of the liquid phase sample were recorded on a Bruker Avance III HD NMR 600 MHz spectrometer equipped with a 5 mm BBO Prodigy cryo‐probe (Bruker BioSpin GmbH, Ettlingen Germany. The sample was dissolved in 600 μl of H₂O, containing 10 % D₂O. 1D 1H with presaturation and 2D homo‐ and heteronuclear NMR experiments (COSY, HSQC, HMBC1) were recorded at 300 K. For acquisition, processing, and evaluation of NMR spectra, the software TopSpin 3.5pl7 (Bruker) was used.

Alhnidi M., Körner P., Wüst D., Pfersich J, & Kruse A. (2020). Nitrogen‐Containing Hydrochar: The Influence of Nitrogen‐Containing Compounds on the Hydrochar Formation. ChemistryOpen, 9(8), 864-873.

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NMR Characterization of GBSIII Polysaccharide

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The GBSIII polysaccharide sample (10 mg) was lyophilized and exchanged twice with 99.9% D

_{2}

O (Sigma Aldrich, Pty. Ltd., Johannesburg, South Africa), then dissolved in 600

μ

L of D

_{2}

O and introduced into a 5 mm NMR tube for data acquisition. 1D

^{1}

H and

^{13}

C and 2D, COSY, TOCSY, NOESY, HSQC, HMBC and hybrid HSQC-TOCSY and HSQC-NOESY spectra were obtained using a Bruker Avance III 600 MHz NMR spectrometer (Bruker BioSpin AG, Fällanden, Switzerland) equipped with a BBO Prodigy cryoprobe and processed using standard Bruker software (Topspin 3.2). The probe temperature was set at 343 K. The 2D TOCSY experiment was performed using a mixing time of 180 ms and the 1D variants using a mixing time of 200 ms. The 2D NOESY experiment was performed using a mixing times of 300 and 500 ms and the 1D variants using mixing times of 300, 400 and 500 ms. The

^{1}

H-

^{13}

C HSQC and HMBC experiments were optimized for J = 145 Hz and 8 Hz, and the HSQC-TOCSY and HSQC-NOESY experiments were recorded using mixing times of 120 and 250 ms, respectively. 2D experiments were recorded using non-uniform sampling: 50% for homonuclear and 25% for heteronuclear experiments. Spectra were referenced relative to the H3ax/C3 signal of terminal sialic acid:

^{1}

H at 1.79 ppm and

^{13}

C at 40.68 ppm [42 (link)].

Kuttel M.M, & Ravenscroft N. (2019). Conformation and Cross-Protection in Group B Streptococcus Serotype III and Streptococcus pneumoniae Serotype 14: A Molecular Modeling Study. Pharmaceuticals, 12(1), 28.

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