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Updated: Jul 18, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
Published on: December 12, 2013
Elimination of 13Calpha splitting in protein NMR spectra by deconvolution with maximum entropy reconstruction
Nobuhisa Shimba1, Alan S Stern, Charles S Craik
1Department of Pharmaceutical Chemistry, University of California-San Francisco, San Francisco, CA 94143, USA.
Abstract:
Homonuclear 13C-13C couplings can significantly reduce the sensitivity and resolution of multidimensional NMR experiments. The most important of these couplings is the 13Calpha-13Cbeta coupling, and several different methods have been developed to eliminate its effect from spectra used for backbone assignment, including short or constant-time evolution periods, selectively labeled amino acids, and multiple-band decoupling sequences. In this communication we show that postacquisition deconvolution of the spectra with a maximum entropy algorithm can be superior to experimental decoupling. The method is very robust, does not introduce shifts of the resonance positions, and simplifies the measurement of the most important NMR experiments for protein backbone assignment.
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