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Zgesgp

Manufactured by Bruker
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The Zgesgp is a specialized lab equipment designed for scientific research and analysis. It serves as a core function to perform specific tasks within the laboratory setting. Further details on its intended use are not available.

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Lab products found in correlation

Hsqcetfpgpsi2, by Bruker (2 mentions) Cd3od, by Merck Group (2 mentions) Topspin 1, by Bruker (2 mentions) Cd3oh, by Cambridge Isotopes (2 mentions) Vnmrj 3.2a, by Bruker (2 mentions) Mestrenova 8, by Bruker (2 mentions) Dipsi2esgpph, by Bruker (2 mentions) Noesyesgpph, by Agilent Technologies (2 mentions) Vnmrs 750, by Agilent Technologies (2 mentions) Hsqcedetgpsisp2, by Bruker (2 mentions) Avance 900, by Bruker (2 mentions) Avance 3, by Bruker (1 mentions)

Close spelling variants of this product

Zgesgp pulse sequence (6 citations) Zgesgp” excitation sculpting water suppression pulse sequence (3 citations) ZGESGP pulse program (3 citations) 1h ZGESGP (2 citations)

6 protocols using zgesgp

1

NMR Analysis of Aβ40 Fibrils with APP-C31

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The solution of fibrillar Aβ40 was prepared by incubation of freshly prepared Aβ40 (200 µm) for 40 h at 37 °C with constant agitation (250 rpm) in 20 mm HEPES, pH 7.4. Aβ40 fibrils were further diluted to be 100 µm in the buffered solution (20 mm HEPES, pH 7.4) containing 10% v/v D2O and then added with APP‐C31 (20 µm). A standard pulse sequence with water suppression by excitation sculpting (zgesgp from Bruker Topspin using the standard parameter set) was used. For each spectrum, 128 transients were collected into 32,768 data points over a spectrum width of 20 ppm. Data were analyzed using TopSpin 3.6.1 software.[87 (link)
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Nam E., Lin Y., Park J., Do H., Han J., Jeong B., Park S., Lee D.Y., Kim M., Han J., Baik M., Lee Y, & Lim M.H. (2023). APP‐C31: An Intracellular Promoter of Both Metal‐Free and Metal‐Bound Amyloid‐β40 Aggregation and Toxicity in Alzheimer's Disease. Advanced Science, 11(4), 2307182.
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2

NMR Spectroscopy of Organic Compounds

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All NMR spectra were recorded on a Bruker 600 MHz Avance II+ at 298 K equipped with a Prodigy TCI probe. One-dimensional 1H-NMR spectra were acquired with excitation sculpting for solvent suppression (Bruker pulse program: zgesgp), recording 512 scans.Two-dimensional 1H-13C-HSQC NMR spectra were recorded using a phase-sensitive ge-2D HSQC with water flip-back pulses and PEP with gradients in back-INEPT (Bruker pulse program hsqcetfpgpsi2): number of scans 72, spectral width in proton dimension 10 ppm, spectral width in carbon dimension 20 ppm, 2048×32 complex data points, 1J(1H,13C) = 200 Hz, interscan delay 1.0 s yielding an acquisition time of approx. 30 minutes per HSQC spectrum.
Ren A., Vušurović N., Gebetsberger J., Gao P., Juen M., Kreutz C., Micura R, & Patel D.J. (2016). Pistol ribozyme adopts a pseudoknot fold facilitating site-specific in-line cleavage. Nature chemical biology, 12(9), 702-708.
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3

NMR Spectroscopy of Organic Compounds

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All NMR spectra were recorded on a Bruker 600 MHz Avance II+ at 298 K equipped with a Prodigy TCI probe. One-dimensional 1H-NMR spectra were acquired with excitation sculpting for solvent suppression (Bruker pulse program: zgesgp), recording 512 scans.Two-dimensional 1H-13C-HSQC NMR spectra were recorded using a phase-sensitive ge-2D HSQC with water flip-back pulses and PEP with gradients in back-INEPT (Bruker pulse program hsqcetfpgpsi2): number of scans 72, spectral width in proton dimension 10 ppm, spectral width in carbon dimension 20 ppm, 2048×32 complex data points, 1J(1H,13C) = 200 Hz, interscan delay 1.0 s yielding an acquisition time of approx. 30 minutes per HSQC spectrum.
Ren A., Vušurović N., Gebetsberger J., Gao P., Juen M., Kreutz C., Micura R, & Patel D.J. (2016). Pistol ribozyme adopts a pseudoknot fold facilitating site-specific in-line cleavage. Nature chemical biology, 12(9), 702-708.
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4

Characterization of Purified Samples by NMR

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HPLC-purified and lyophilized samples (ca. 1–5 mg) were dissolved in 600 µL of CD3OD (99.96 atom % D; Sigma-Aldrich) or CD3OH (99.5 atom % D; Cambridge Isotope Labs). Spectra were obtained with either a Bruker AVANCE 900 MHz narrow bore spectrometer equipped with an inverse 5 mm TCI cryogenic probe with z-axis pulsed field gradient (pfg) capability or on an Agilent VNMRS 750 MHz narrow bore magnet spectrometer equipped with a 5 mm triple resonance (1H-13C-15N) triaxial gradient probe and pulse-shaping capabilities. Samples were held at 298 K during acquisition. Standard Bruker or Varian pulse sequences were used for each of the following experiments: 1H, 1H with solvent suppression using excitation sculpting (Bruker: zgesgp), 1H-1H TOCSY (80 ms mixing time; Bruker: dipsi2esgpph), 1H-13C HSQC (multiplicity-edited; Bruker: hsqcedetgpsisp2), and 1H-1H NOESY (400 ms mixing time; Bruker: noesyesgpph; Varian: dpfgse_noesy). 2D spectra in CD3OH employed solvent suppression as per the listed pulse sequences. Spectra were recorded with Bruker TopSpin 1.3 or VNMRJ 3.2A software, and data was processed using MestReNova 8.1.1. Chemical shifts (δ, ppm) were referenced internally to the solvent peak. All NMR data are shown in Supplementary Figure 15.
Tietz J.I., Schwalen C.J., Patel P.S., Maxson T., Blair P.M., Tai H.C., Zakai U.I, & Mitchell D.A. (2017). A new genome-mining tool redefines the lasso peptide biosynthetic landscape. Nature chemical biology, 13(5), 470-478.
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5

Characterization of Purified Samples by NMR

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HPLC-purified and lyophilized samples (ca. 1–5 mg) were dissolved in 600 µL of CD3OD (99.96 atom % D; Sigma-Aldrich) or CD3OH (99.5 atom % D; Cambridge Isotope Labs). Spectra were obtained with either a Bruker AVANCE 900 MHz narrow bore spectrometer equipped with an inverse 5 mm TCI cryogenic probe with z-axis pulsed field gradient (pfg) capability or on an Agilent VNMRS 750 MHz narrow bore magnet spectrometer equipped with a 5 mm triple resonance (1H-13C-15N) triaxial gradient probe and pulse-shaping capabilities. Samples were held at 298 K during acquisition. Standard Bruker or Varian pulse sequences were used for each of the following experiments: 1H, 1H with solvent suppression using excitation sculpting (Bruker: zgesgp), 1H-1H TOCSY (80 ms mixing time; Bruker: dipsi2esgpph), 1H-13C HSQC (multiplicity-edited; Bruker: hsqcedetgpsisp2), and 1H-1H NOESY (400 ms mixing time; Bruker: noesyesgpph; Varian: dpfgse_noesy). 2D spectra in CD3OH employed solvent suppression as per the listed pulse sequences. Spectra were recorded with Bruker TopSpin 1.3 or VNMRJ 3.2A software, and data was processed using MestReNova 8.1.1. Chemical shifts (δ, ppm) were referenced internally to the solvent peak. All NMR data are shown in Supplementary Figure 15.
Tietz J.I., Schwalen C.J., Patel P.S., Maxson T., Blair P.M., Tai H.C., Zakai U.I, & Mitchell D.A. (2017). A new genome-mining tool redefines the lasso peptide biosynthetic landscape. Nature chemical biology, 13(5), 470-478.
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6

Biomolecular Interactions: NMR Analysis

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PAsmr was purified as described above. Binding of MeTPP+ and streptomycin was assessed by 1H NMR. Samples contained 500 μM MeTPP+ or streptomycin with or without 25 μM PAsmr in DHPC/DMPC bicelles, in a buffer of 20 mM NaCl, 20 mM potassium phosphate, 8% D2O, and 0.3 mM sodium trimethylsilylpropanesulfonate (DSS) at pH 7. Samples containing protein also contained 0.05% sodium azide and 2 mM tris (2-carboxyethyl)phosphine (TCEP). All spectra were acquired on a Bruker Avance III spectrometer operating at 600 MHz. 1D spectra were acquired using the Bruker pulse program zgesgp. WaterLOGSY experiments were recorded at specified temperatures using the Bruker pulse program ephogsygpno.2 with a mixing time of 1.5 s and 2 s recycle delay. All spectra were processed and visualized with Mnova.
Wegrzynowicz A.K., Heelan W.J., Demas S.P., McLean M.S., Peters J.M, & Henzler-Wildman K.A. (2024). A Small Multidrug Resistance Transporter in Pseudomonas aeruginosa Confers Substrate-Specific Resistance or Susceptibility. bioRxiv.
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