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Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
13:59

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins

Published on: December 12, 2013

NMR determination of residual structure in a urea-denatured protein, the 434-repressor

D Neri1, M Billeter, G Wider

  • 1Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, Zürich, Switzerland.

Science (New York, N.Y.)
|September 11, 1992
PubMed

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The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...