DURING THE LAST FEW YEARS high‐resolution nuclear magnetic‐resonance (NMR) spectroscopy has become a powerful technique for investigating the molecular and electronic structure of biological compounds. The high sensitivity and resolution of recently developed spectrometers with superconducting solenoids has made possible many new applications and has yielded data not obtainable by other methods. NMR experiments can be done under conditions similar to the physiological environment of the molecules: in aqueous solution and at body temperature. Thus with NMR it is often possible to establish relations between data on the structure of biological compounds in the solid state, obtained by techniques like x‐ray crystallography, and the corresponding molecular properties in solution.
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April 1970
April 01 1970
Magnetic resonance in biology
High‐resolution proton nuclear magnetic‐resonance spectroscopy leads to new insights in structure–function relations in heme proteins.
Kurt Wüthrich;
Kurt Wüthrich
Institute of Molecular Biology and Biophysics, ETH, Zürich, Switzerland
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Robert G. Shulman
Robert G. Shulman
Biophysical Research Department, Bell Telephone Laboratories, Murray Hill, New Jersey
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Physics Today 23 (4), 43–50 (1970);
Citation
Kurt Wüthrich, Robert G. Shulman; Magnetic resonance in biology. Physics Today 1 April 1970; 23 (4): 43–50. https://doi.org/10.1063/1.3022065
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