Log In Sign up
The largest database of trusted experimental protocols

Vnmrj 3.2a

Manufactured by Bruker
Visit Supplier

VNMRJ 3.2A is a nuclear magnetic resonance (NMR) software package developed by Bruker. It provides a user interface and tools for controlling and analyzing NMR experiments. The core function of VNMRJ 3.2A is to enable the acquisition, processing, and visualization of NMR data.

Automatically generated - may contain errors

Lab products found in correlation

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

2 protocols using vnmrj 3.2a

1

Characterization of Purified Samples by NMR

Check if the same lab product or an alternative is used in the 5 most similar protocols
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.
+ Open protocol
+ Expand
2

Characterization of Purified Samples by NMR

Check if the same lab product or an alternative is used in the 5 most similar protocols
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.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!