Reductive Methylation

PRE NMR and reductive 13C-methylation to study protein quaternary structure

Our group has studied protein reductive 13C-methlation as a tool for NMR analysis and developed methods to assign the NMR peaks of reductively 13C-methylated proteins with the support of an NIH K99 and R00 award.

Related Publications

  1. P. N. Brady and M. A. Macnaughtan, Evaluation of colorimetric assays for analyzing reductively methylated proteins: Biases and mechanistic insights. Analytical Biochemistry, 2015, 491, 43-51. 
  2. K. J. Roberson and M. A. Macnaughtan, Review: Methods to assign NMR resonances from reductively methylated proteins. Analytical Biochemistry, 2014, 466, 76-82.
  3. K. J. Roberson and M. A. Macnaughtan, Attempts towards unambiguously assigning 13C-dimethylamine NMR resonances, The All Results Journal: Chemistry. 2013, 4, 10-16.
  4. K. J. Roberson, P. N. Brady, M. M. Sweeney, and M. A. Macnaughtan, Methods to identify the NMR resonances of the 13C-dimethyl N-terminal amine on reductively methylated proteins. Journal of Visualized Experiments, 2013, 82, e50875. Video.
  5. M. A. Macnaughtan, A. Kane, and J. H. Prestegard, Mass spectrometry assisted assignment of NMR resonances in 13C-reductively methylated proteins, Journal of the American Chemical Society, 2005, 127, 17626-17627.