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Natural Abundance Fourier Transform of 13C Nuclear Magnetic Resonance Spectra of Lysozyme

Abstract

NUCLEAR magnetic resonance (NMR) studies of biopolymers have so far been limited to proton resonances. On the other hand, 13C NMR analysis is potentially a more powerful technique because of the larger range of chemical shifts (300 p.p.m. compared with 10 p.p.m. for XH NMR), and because the chemical shift of 13C NMR is more sensitive to the nature of the chemical bonds. The chief limitations of 13C NMR are low natural abundance (1·1%), low relative sensitivity (1·59% of proton), and long relaxation times (˜1 min). These can be largely overcome, however, by the combined techniques of nuclear Overhauser enhancement and fourier transform spectroscopy. Thus, Gibbons et al.1 obtained a simple and elegant spectral analysis of ‘Gramicidin S-A’, a decapeptide. We report here the first natural abundance 13C NMR spectrum of an enzyme. Lysozyme was chosen because its primary structure is known2,3 and because its 1H NMR spectrum has already been described4.

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CHIEN, J., BRANDTS, J. Natural Abundance Fourier Transform of 13C Nuclear Magnetic Resonance Spectra of Lysozyme. Nature New Biology 230, 209–210 (1971). https://doi.org/10.1038/newbio230209a0

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