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  2. Nuclear magnetic resonance spectroscopy of carbohydrates

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

    Carbohydrate NMR spectroscopy is the application of nuclear magnetic resonance (NMR) spectroscopy to structural and conformational analysis of carbohydrates.This method allows the scientists to elucidate structure of monosaccharides, oligosaccharides, polysaccharides, glycoconjugates and other carbohydrate derivatives from synthetic and natural sources.

  3. Nuclear magnetic resonance crystallography - Wikipedia

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

    The “dipole coupling”-based approach parallels protein NMR spectroscopy to some extent in that e.g. multiple residual dipolar couplings are measured for proteins in solution, and these couplings are used as constraints in the protein structure calculation. In NMR crystallography the observed spins in case of organic molecules would often be ...

  4. Karplus equation - Wikipedia

    en.wikipedia.org/wiki/Karplus_equation

    where J is the 3 J coupling constant, is the dihedral angle, and A, B, and C are empirically derived parameters whose values depend on the atoms and substituents involved. [3] The relationship may be expressed in a variety of equivalent ways e.g. involving cos 2φ rather than cos 2 φ —these lead to different numerical values of A , B , and C ...

  5. Nuclear magnetic resonance decoupling - Wikipedia

    en.wikipedia.org/wiki/Nuclear_Magnetic_Resonance...

    Only these isotopes cause NMR coupling. Nuclei of atoms having the same equivalent positions within a molecule also do not couple with each other. 1 H (proton) NMR spectroscopy and 13 C NMR spectroscopy analyze 1 H and 13 C nuclei, respectively, and are the most common types (most common analyte isotopes which show signals) of NMR spectroscopy.

  6. Magnetic inequivalence - Wikipedia

    en.wikipedia.org/wiki/Magnetic_inequivalence

    In molecules of uncertain or otherwise unproven structure, the definitive appearance of complexity in a pair of signals, beyond what can be explained by first-order analysis of HC-CH pairs or H 2 C-CH 2 fragments, can be taken to signify the presence of magnetic inequivalence and, therefore, of an element of symmetry aggregating them.

  7. Residual dipolar coupling - Wikipedia

    en.wikipedia.org/wiki/Residual_dipolar_coupling

    Most NMR studies of protein structure are based on analysis of the Nuclear Overhauser effect, NOE, between different protons in the protein. Because the NOE depends on the inverted sixth power of the distance between the nuclei, r −6 , NOEs can be converted into distance restraints that can be used in molecular dynamics -type structure ...

  8. Two-dimensional nuclear magnetic resonance spectroscopy

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

    In 2D NMR, signals are distributed across two frequency axes, providing improved resolution and separation of overlapping peaks, particularly beneficial for studying complex molecules. This technique identifies correlations between different nuclei within a molecule, facilitating the determination of connectivity, spatial proximity, and dynamic ...

  9. Nuclear magnetic resonance spectroscopy - Wikipedia

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

    Besides identification, NMR spectroscopy provides detailed information about the structure, dynamics, reaction state, and chemical environment of molecules. The most common types of NMR are proton and carbon-13 NMR spectroscopy, but it is applicable to any kind of sample that contains nuclei possessing spin.