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
- 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.
- K. J. Roberson and M. A. Macnaughtan, Review: Methods to assign NMR resonances from reductively methylated proteins. Analytical Biochemistry, 2014, 466, 76-82.
- K. J. Roberson and M. A. Macnaughtan, Attempts towards unambiguously assigning 13C-dimethylamine NMR resonances, The All Results Journal: Chemistry. 2013, 4, 10-16.
- 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.
- 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.