Magnetic resonance in biology

APR 01, 1970

High‐resolution proton nuclear magnetic‐resonance spectroscopy leads to new insights in structure–function relations in heme proteins.

DOI: 10.1063/1.3022065

Kurt Wüthrich

Robert G. Shulman

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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References

1. F. A. Nelson, H. E. Weaver, Science 146, 223 (1964).https://doi.org/SCIEAS
2. F. A. Bovey, Chem. Eng. News 43, no. 35, 98 (1965).
3. C. C. McDonald, W. D. Phillips, Biological Macromolecules, Vol. III, G. D. Fasman, S. N. Timasheff, eds. “Proton Magnetic Resonance Spectroscopy of Proteins” (to be published).
4. G. C. K. Roberts, O. Jardetzky, Adv. in Protein Chemistry (in press).
“Nuclear Magnetic Resonance Spectroscopy of Amino Acids, Peptides, and Proteins.”
5. For more detailed accounts of our investigations of heme proteins see Proc. Nat. Acad. Sci. U.S., 60, 373 (1968);
61, 1199 (1968);
62, 637 (1969);
Science 165, 251 (1969).

More about the Authors

Kurt Wüthrich. Institute of Molecular Biology and Biophysics, ETH, Zürich, Switzerland.

Robert G. Shulman. Biophysical Research Department, Bell Telephone Laboratories, Murray Hill, New Jersey.