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  2. Proton nuclear magnetic resonance - Wikipedia

    en.wikipedia.org/wiki/Proton_nuclear_magnetic...

    Proton nuclear magnetic resonance (proton NMR, hydrogen-1 NMR, or 1 H NMR) is the application of nuclear magnetic resonance in NMR spectroscopy with respect to hydrogen-1 nuclei within the molecules of a substance, in order to determine the structure of its molecules. [1]

  3. Isotopic analysis by nuclear magnetic resonance - Wikipedia

    en.wikipedia.org/wiki/Isotopic_analysis_by...

    2 H-SNIF-NMR is the official AOAC method for determining the natural vanillin. The abundance of five monodeuterated isotopomers for vanillin can be measured by 2 H-SNIF-NMR. The vanillin molecule is represented in figure 11, all observable sites for which the site specific deuterium concentrations can be measured are referenced with a number.

  4. Nuclear magnetic resonance spectra database - Wikipedia

    en.wikipedia.org/wiki/Nuclear_magnetic_resonance...

    Available through Wiley Online Library [3] (John Wiley & Sons), SpecInfo on the Internet NMR is a collection of approximately 440,000 NMR spectra (organized as 13 C, 1 H, 19 F, 31 P, and 29 Si NMR databases). The data are accessed via the Internet using a Java interface and are stored in a server developed jointly with BASF. The software ...

  5. Isotopic shift - Wikipedia

    en.wikipedia.org/wiki/Isotopic_shift

    H NMR spectrum of a solution of HD (labeled with red bars) and H 2 (blue bar). The 1:1:1 triplet arises from the coupling of the 1 H nucleus (I = 1/2) to the 2 H nucleus (I = 1). In NMR spectroscopy, isotopic effects on chemical shifts are typically small, far less than 1 ppm, the typical unit for measuring shifts. The 1 H NMR signals for 1 H 2 ...

  6. Triple-resonance nuclear magnetic resonance spectroscopy

    en.wikipedia.org/wiki/Triple-resonance_nuclear...

    Triple resonance experiments are a set of multi-dimensional nuclear magnetic resonance spectroscopy (NMR) experiments that link three types of atomic nuclei, most typically consisting of 1 H, 15 N and 13 C. These experiments are often used to assign specific resonance signals to specific atoms in an isotopically-enriched protein.

  7. Paramagnetic nuclear magnetic resonance spectroscopy

    en.wikipedia.org/wiki/Paramagnetic_nuclear...

    Paramagnetism diminishes the resolution of an NMR spectrum to the extent that coupling is rarely resolved. Nonetheless spectra of paramagnetic compounds provide insight into the bonding and structure of the sample. For example, the broadening of signals is compensated in part by the wide chemical shift range (often 200 ppm in 1 H NMR).

  8. Two-dimensional nuclear magnetic resonance spectroscopy

    en.wikipedia.org/wiki/Two-dimensional_nuclear...

    While 1D NMR is more straightforward and ideal for identifying basic structural features, COSY enhances the capabilities of NMR by providing deeper insights into molecular connectivity. The two-dimensional spectrum that results from the COSY experiment shows the frequencies for a single isotope , most commonly hydrogen ( 1 H) along both axes.

  9. Nuclear magnetic resonance spectroscopy of carbohydrates

    en.wikipedia.org/wiki/Nuclear_magnetic_resonance...

    Typical 1 H NMR chemical shifts of carbohydrate ring protons are 3–6 ppm (4.55.5 ppm for anomeric protons). Typical 13 C NMR chemical shifts of carbohydrate ring carbons are 60–110 ppm In the case of simple mono- and oligosaccharide molecules, all proton signals are typically separated from one another (usually at 500 MHz or better NMR ...

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