[Home]History of Nuclear Magnetic Resonance

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Revision 23 . . (edit) September 23, 2001 11:32 pm by Sodium
Revision 22 . . (edit) August 5, 2001 1:04 am by IowaStateUniversity
Revision 19 . . August 5, 2001 12:48 am by IowaStateUniversity [*put in "see also" section, removed wiki-redundant "back to physics" link]
  

Difference (from prior major revision) (minor diff, author diff)

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Nuclear Magnetic Resonance (NMR)

Physical phenomenon described independently by [F. Bloch]? and [E. M. Purcell]? in 1946 both of whom shared the Nobel Prize in physics in 1952 for their discovery. It involves the interaction of atomic nucleus placed in an external magnetic field with applied electro-magnetic field oscillating at a particular frequency. At that frequency, energy from the electro-magnetic field can be absorbed by the nucleus.
Nuclear Magnetic Resonance (NMR) is a physical phenomenon described independently by [F. Bloch]? and [E. M. Purcell]? in 1946 both of whom shared the Nobel Prize in physics in 1952 for their discovery. It involves the interaction of atomic nucleus placed in an external magnetic field with applied electro-magnetic field oscillating at a particular frequency. At that frequency, energy from the electro-magnetic field can be absorbed by the nucleus.

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[Kurt Wutrich]?, [Ad Bax]? and many others, developed FT-NMR into a powerful technique for studying biochemistry, in particular for the determination of the structure of biopolymers such as proteins or even small nucleic acids. This technique complements biopolymer X-ray crystallography in that it is most frequently applicable to biomolecules in a liquid or liquid crystal phase, whereas crystallography (as the name implies) is performed on molecules in a solid phase.
[Kurt Wutrich]?, [Ad Bax]? and many others, developed FT-NMR into a powerful technique for studying biochemistry, in particular for the determination of the structure of biopolymers such as proteins or even small nucleic acids. This technique complements biopolymer X-ray crystallography in that it is most frequently applicable to biomolecules in a liquid or liquid crystal phase, whereas crystallography (as the name implies) is performed on molecules in a solid phase. Though NMR is used to study solids, extensive atomic-level biomolecular structural detail is especially difficult to obtain in the solid state.

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The sensitivity of NMR signals is also dependent, as noted above, on the presence of a magnetically-susceptible isotope, and therefore either on the natural abundance of such isotopes, or on the ability of the experimentalist to artificially enrich the molecules under study with such isotopes. The most abundant naturally occuring isotopes of hydrogen and phosphorus, for instance, are both magneticallys susceptible and readily useful for NMR spectroscopy. In contrast, carbon and nitrogen have useful nuclei, but which occur only in very low natural abundance.
The sensitivity of NMR signals is also dependent, as noted above, on the presence of a magnetically-susceptible isotope, and therefore either on the natural abundance of such isotopes, or on the ability of the experimentalist to artificially enrich the molecules under study with such isotopes. The most abundant naturally occuring isotopes of hydrogen and phosphorus, for instance, are both magnetically susceptible and readily useful for NMR spectroscopy. In contrast, carbon and nitrogen have useful nuclei, but which occur only in very low natural abundance.

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*electromagnetism

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