One of the questions that we always get at tradeshows and conferences is how our instrument compares to high-field data. There are significant inherent differences between low-field and high-field instruments, but the most important from a chemistry point of view are sensitivity (S/N) and resonance dispersion (signal separation). Read More.

In this blog post, I will talk about how to select a suitable calibrant as well as the difference between using an internal and external calibrant. When conducting qNMR experiments, one of the first things that needs to be considered is how the calibrant is employed to quantitate your sample. Read more.

Symmetry is beauty. There are countless examples in nature, just think about honeycombs, flowers, starfish or….maleic acid! You probably can guess which of these examples will be the star in this blog post - no, sorry, it is not the starfish…

Over the last few years, more and more analytical and industrial laboratories have started employing quantitative nuclear magnetic resonance (qNMR) spectroscopy as a tool for content assignment (due to its superb structural elucidation abilities) and quantification of purity in a sample. Read more.

NMR users can deal with spectrum evaluation in the daily work, but how is the spectrum information stored in the time domain (FID)? Read more.

Nuclear Magnetic Resonance spectroscopy is based on the idea that some nuclei can behave as little magnetic bars (I spin number ≠ 0). In the presence of a magnetic field (B0) the nuclear spins feel a small torque for or against the B0 axis, which results in a net magnetization along the B0 direction. Benchtop NMR 1-855-NMREADY (667-3239) toll-free in the US and Canada.

Hello fellow NMR enthusiasts, have you ever wondered what tritium (3H) looks like via NMR? I know I have, and today, I would like to share some data with you. Read noww.

NMR is a great tool for the analysis of molecular properties such as the amide bond, which has a restricted rotation around the C–N bond. In Biochemistry, the amide bond is referred to as the peptide bond. This bond is formed by the union of a carboxyl group of one amino acid with the amino group of another amino acid. Read more.

Distortionless Enhancement by Polarization Transfer (DEPT) is a double resonance pulse program that transfers polarization from an excited nucleus to another – most commonly 1H → 13C. This results in a sensitivity enhancement relative to the standard decoupled 1D carbon spectra (13C), which benefits only from the small Nuclear Overhauser Effect (NOE) enhancements.

Have you ever questioned why hydroxyl groups/alcohol signals appear as singlet in the 1H NMR spectrum? Shouldn’t they also couple with neighboring hydrogen atoms and show the corresponding splitting pattern? Yes…no…why? Don’t worry! We’ll get to the bottom of it and discuss how exchange rates, concentrations, and the presence of water affect the NMR spectra of ethanol in CDCl3. Benchtop NMR solves so many questions – feel free to reach out to us to make sure yours can answered too.