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1.7 mm cryogenic probe

Manufactured by Bruker
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The 1.7-mm cryogenic probe is a lab equipment product designed for use in nuclear magnetic resonance (NMR) spectroscopy. It provides a compact and sensitive solution for conducting NMR experiments at cryogenic temperatures, which can enhance the signal-to-noise ratio and resolution of NMR spectra.

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Lab products found in correlation

Advance 600 mhz nmr spectrometer, by Bruker (1 mentions) Zgesgp pulse program, by Bruker (1 mentions)

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Cryogenic probe (39 citations)

3 protocols using 1.7 mm cryogenic probe

1

NMR Characterization of Tryptophan Zipper Peptides

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NMR spectra of peptides were acquired with an Avance III 600 MHz spectrometer equipped with a 1.7-mm cryogenic probe from Bruker in the NMRFAM. As described previously29 (link), TrpZip peptides were dissolved to a final concentration of ~1 mM in 40 μL of 20 mM potassium phosphate buffer, pH 7.0, containing 10% v/v D2O. Homonuclear ROESY, COSY, and TOCSY spectra were collected at 25 °C with water suppression, and resonances were assigned by standard methods. Specifically, sequential Hαi–NHi+1 ROESY correlations provided connectivities and confirmed the β-like backbone geometry.
Newberry R.W, & Raines R.T. (2016). A prevalent intraresidue hydrogen bond stabilizes proteins. Nature chemical biology, 12(12), 1084-1088.
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2

NMR Characterization of Tryptophan Zipper Peptides

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NMR spectra of peptides were acquired with an Avance III 600 MHz spectrometer equipped with a 1.7-mm cryogenic probe from Bruker in the NMRFAM. As described previously29 (link), TrpZip peptides were dissolved to a final concentration of ~1 mM in 40 μL of 20 mM potassium phosphate buffer, pH 7.0, containing 10% v/v D2O. Homonuclear ROESY, COSY, and TOCSY spectra were collected at 25 °C with water suppression, and resonances were assigned by standard methods. Specifically, sequential Hαi–NHi+1 ROESY correlations provided connectivities and confirmed the β-like backbone geometry.
Newberry R.W, & Raines R.T. (2016). A prevalent intraresidue hydrogen bond stabilizes proteins. Nature chemical biology, 12(12), 1084-1088.
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3

NMR Characterization of Purified Metabolite

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NMR experiments were performed on a Bruker Advance 600-MHz NMR spectrometer equipped with a 1.7 mm cryogenic probe.
The 1 H NMR water signal from the polar fraction was suppressed by means of excitation sculpting (Bruker ZGESGP pulse program). Additional 13 C NMR spectra were acquired for each sample. 1 H-1 H COSY, 1 H-13 C HSQC, 1 H-13 C HMBC and 1 H-15 N HMBC experiments was only carried out for the purified metabolite sample.
Chemical shifts (expressed in ppm) of 1 H NMR spectra were referenced to the solvent peaks δ H 4.79 for D 2 O.
3-((3-Aminopropyl)amino)-4-hydroxybenzoic acid (M211; APAH):
Thomas M., Stuani L., Darii E., Lechaplais C., Pateau E., Tabet J., Salanoubat M., Saaidi P., & Perret A. (2019). De novo structure determination of 3-((3-aminopropyl)amino)-4-hydroxybenzoic acid, a novel and abundant metabolite in Acinetobacter baylyi ADP1. Metabolomics, 15(3).
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