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A 900 MHz NMR instrument with a 21.1 T magnet at HWB-NMR, Birmingham, UK. Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique based on re-orientation of atomic nuclei with non-zero nuclear spins in an external magnetic field.
One important problem using homonuclear nuclear magnetic resonance is overlap between peaks. This occurs when different protons have the same or very similar chemical shifts. This problem becomes greater as the protein becomes larger, so homonuclear nuclear magnetic resonance is usually restricted to small proteins or peptides. [citation needed]
In solid-state NMR spectroscopy, magic-angle spinning (MAS) is a technique routinely used to produce better resolution NMR spectra. MAS NMR consists in spinning the sample (usually at a frequency of 1 to 130 kHz) at the magic angle θ m (ca. 54.74°, where cos 2 θ m =1/3) with respect to the direction of the magnetic field.
Solid state NMR (SSNMR), unlike LSNMR uses a solid state sample, for example a nitrogen vacancy diamond lattice rather than a liquid sample. [3] This has many advantages such as lack of molecular diffusion decoherence, lower temperatures can be achieved to the point of suppressing phonon decoherence and a greater variety of control operations that allow us to overcome one of the major problems ...
These problems may be alleviated by using heteronuclear NMR spectroscopy which allows the proton spectrum to be edited with respect to the 15 N and 13 C chemical shifts, and also reduces the overlap of resonances by increasing the number of dimensions of the spectrum.
Solid-state 900 MHz (21.1 T [1]) NMR spectrometer at the Canadian National Ultrahigh-field NMR Facility for Solids. Solid-state nuclear magnetic resonance (ssNMR) is a spectroscopy technique used to characterize atomic-level structure and dynamics in solid materials. ssNMR spectra are broader due to nuclear spin interactions which can be categorized as dipolar coupling, chemical shielding ...
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]
The 19 F NMR chemical shifts span a range of about 800 ppm. For organofluorine compounds the range is narrower, being about −50 to −70 ppm (for CF 3 groups) to −200 to −220 ppm (for CH 2 F groups). The very wide spectral range can cause problems in recording spectra, such as poor data resolution and inaccurate integration.
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