Avance 2 900 mhz spectrometer

Manufactured by Bruker

The Avance II 900 MHz spectrometer is a high-resolution nuclear magnetic resonance (NMR) instrument designed for advanced analytical applications. It operates at a frequency of 900 MHz, providing exceptional spectral resolution and sensitivity for the structural elucidation and characterization of complex molecular systems.

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Lab products found in correlation

Cryogenic probe, by Bruker (2 mentions) Topspin, by Bruker (1 mentions) Xl 1 analytical ultracentrifuge, by Beckman Coulter (1 mentions)

Close spelling variants of this product

Avance spectrometer (419 citations) Avance II (229 citations) Bruker spectrometers (71 citations) Avance II spectrometer (58 citations) 900 MHz spectrometer (24 citations) Avance 900 MHz spectrometer (11 citations) Avance 900 (8 citations) Avance 900 MHz (4 citations) Avance II 900 (4 citations) Avance 900 spectrometer (3 citations)

3 protocols using avance 2 900 mhz spectrometer

NMR Structural Analysis of G-Quadruplex-Protein Interactions

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NMR experiments were performed using
a Bruker Avance II 900 MHz spectrometer equipped with a cryogenic
probe (Korea Basic Science Institute, Ochang). 1D proton spectra of
0.3 mM hTelo-3nt G4 were obtained at 25 °C. ¹H–¹⁵N HSQC spectra of 0.3 mM ¹⁵N-labeled RQC in the
absence or presence of G4s were also obtained at 25 °C. All NMR
data were processed with Topspin (Bruker) and analyzed with SPARKY
software. The following equation was used to calculate the average chemical shift perturbation values
(Δδ_avg). Δδ_avg values
higher than one standard deviation above the average are selected
as the significantly perturbed residues

Lee S., Kim J., Han S, & Park C.J. (2020). Recognition and Unfolding of c-MYC and Telomeric G-Quadruplex DNAs by the RecQ C-Terminal Domain of Human Bloom Syndrome Helicase. ACS Omega, 5(24), 14513-14522.

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NMR Analysis of Protein Structure

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NMR data were collected at 298 K at the NMR Facility at the University of California, Berkeley on Bruker Avance II 900 MHz spectrometer equipped with a Bruker cryogenic probe. HSQC spectra were collected using 1 mM protein at 25°C in a buffer of 20 mM HEPES NaOH pH 7.5, 100 mM potassium chloride, 5% (w/v) glycerol, 1 mM TCEP, and 5% D₂O. Data were processed using NMRpipe and analyzed using NMRviewJ.

Wilson R.C., Tambe A., Kidwell M.A., Noland C.L., Schneider C.P, & Doudna J.A. (2014). Dicer–TRBP complex formation ensures accurate mammalian microRNA biogenesis. Molecular cell, 57(3), 397-407.

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Biophysical Characterization of Proteins

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All experiments were performed at room temperature, with the following buffer conditions: 20 mM sodium acetate, pH 5.5, and 50 mM potassium chloride. CD experiments were measured on an Aviv 410 CD spectropolarimeter in a cuvette with a 1-mm or 1-cm pathlength, as appropriate to the protein concentration. For each construct, at least one equilibrium denaturation was performed after incubating individual samples overnight. The rest were performed with shorter incubations, some using a titrator with a 5-min equilibration time between samples. (The exception is that all samples for the full-length ttRNH variant were incubated overnight.) The results were consistent at all incubation times. 95% confidence intervals are based on the average of 3–5 experiments. NMR experiments were recorded on a Bruker Avance II 900-MHz spectrometer, as described previously [25 (link)]. Equilibrium ultracentrifugation experiments were performed with a Beckman XL-I analytical ultracentrifuge, as described previously [25 (link)].

Rosen L.E, & Marqusee S. (2015). Autonomously Folding Protein Fragments Reveal Differences in the Energy Landscapes of Homologous RNases H. PLoS ONE, 10(3), e0119640.

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