Abstract
NATIVE proteins in solution usually give rise to nuclear magnetic resonance (NMR) spectra containing broad overlapping bands1–5. These bands contain a great deal of useful information, most of which cannot be extracted without some simplification of the spectra. Selective deuteration is one method for reducing the complexity of macromolecular NMR spectra6,7, but the production of deuterated proteins is not always feasible. NMR difference spectroscopy is simpler, relying on the principle of selective perturbation (by means of change of solvent, pH and so on) of only one or several types of proton resonances in the spectrum. This technique has been used previously to examine differences between the spectra of bovine and porcine insulin8 and to study the binding of Co(II) to the carboxyl groups of gelatine (reported by P. I. Rose at IUPAC symposium on macromolecular chemistry, Toronto, 1968).
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KING, N., BRADBURY, J. Simplification of the Proton Magnetic Resonance Spectrum of Ribonuclease by Difference Spectroscopy. Nature 229, 404–406 (1971). https://doi.org/10.1038/229404a0
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DOI: https://doi.org/10.1038/229404a0
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