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For the wide uses of NMR spectroscopy (from mineralogy to medicine) there is a variety of different spectroscopic imaging techniques available.
A short listing of the most frequent variations:
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'Two-dimensional NMR Spectroscopy' (2D NMR) is based on pulse spectroscopy. This technique is mostly used for the study of chemical interactions accompanied by magnetization transfer. Examples for more diversified spectroscopy techniques are based on homonuclear (COSY, TOCSY, 2D-INADEQUATE, NOESY, ROESY) or heteronuclear correlation (HSQC, HMQC, HMBC).
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'Solid State NMR Spectroscopy' analyzes samples with little or no molecular mobility. Dipolar coupling and chemical shift anisotropy are the dominating nuclear physical effects here. Used for example in pharmaceutical analysis.
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'Solution State NMR Spectroscopy' is a technique to analyze the structure of samples with a high degree of molecular mobility as polymers, proteins, nucleic acids etc.
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Edward Purcell and Felix Bloch discovered the basic of spectroscopy in 1946 (see MRI History). Nuclear magnetic resonance spectroscopy ( NMR Spectroscopy or MRS) is an analytical tool, based on nuclei that have a spin (nuclei with an odd number of neutrons and/or protons) like 1H, 13C, 17O, 19F, 31P etc.
Through nuclear magnetic principles as precession, chemical shift, spin spin coupling etc., the analysis of the content, purity, and molecular structure of a sample is possible. The spectrum produced by this process contains a number of peaks; the highs and the positions of these peaks allow the exact analysis. Unknown compounds can be matched against spectral libraries. Even very complex organic compounds as enzymes and proteins can be determined. For the wide uses of NMR spectroscopy (from mineralogy to medicine) there is a variety of different techniques available.
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