The Application of 1H Nuclear Magnetic Resonance Spectroscopy to the Study of Enzymes

  • Christina Redfield
Part of the Progress in Mathematics book series (NSSA)

Abstract

Nuclear magnetic resonance spectroscopy has been used to study enzymes for more than 30 years. The first 1H NMR spectrum of a protein was published by Saunders, Wishnia and Kirkwood in 1957 1. The 40 MHz spectrum of ribonuclease consisted of 4 broad peaks. The authors assigned the most downfield peak in the spectrum to the aromatic protons and the most upfield peak to hydrogens bonded to aliphatic carbon atoms attached only to other aliphatic carbon. They reported that the intensities of these two peaks were consistent with the amino acid composition of ribonuclease. Later in 1957 Jardetsky and Jardetsky used the chemical shifts of the amino acids to predict a complete NMR spectrum for ribonuclease 2. Their predicted intensities were in good agreement with the intensities of the four peaks in the ribonuclease spectrum, and they concluded that the NMR spectra of amino acids provide a rational basis for the interpretation of the NMR spectra of proteins in solution. Today the complete interpretation of the NMR spectra of proteins is still the goal of many NMR spectroscopists; only the level of detail of this interpretation has changed. The NMR spectra of the amino acid building blocks are still used to interpret complex protein spectra.

Keywords

Cross Peak NOESY Spectrum Cosy Spectrum Sequential Assignment Fingerprint Region 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Christina Redfield
    • 1
  1. 1.Inorganic Chemistry LaboratoryUniversity of OxfordOxfordEngland

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