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Updated: Jun 18, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
Published on: December 12, 2013
Selective 1H- 13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
Chenyun Guo1, Vitali Tugarinov
1Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA.
Abstract:
Methyl (13)CHD(2) isotopomers of all methyl-containing amino-acids can be observed in residually protonated samples of large proteins obtained from [U-(13)C,(1)H]-glucose/D(2)O-based bacterial media, with sensitivity sufficient for a number of NMR applications. Selective detection of some subsets of methyl groups (Ala(beta), Thr(gamma 2)) is possible using simple 'out-and-back' NMR methodology. Such selective methyl-detected 'out-and-back' NMR experiments allow complete assignments of threonine gamma 2 methyls in residually protonated, [U-(13)C,(1)H]-glucose/D(2)O-derived samples of an 82-kDa enzyme Malate Synthase G. [U-(13)C,(1)H]-glucose/D(2)O-derived protein samples are relatively inexpensive and are usually available at very early stages of any NMR study of high-molecular-weight systems.
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