Lysine methylation strategies for characterizing protein conformations by NMR.

@article{Larda2012LysineMS,
  title={Lysine methylation strategies for characterizing protein conformations by NMR.},
  author={Sacha Thierry Larda and Michael P. Bokoch and Ferenc Evanics and Robert Scott Prosser},
  journal={Journal of biomolecular NMR},
  year={2012},
  volume={54 2},
  pages={199-209}
}
In the presence of formaldehyde and a mild reducing agent, reductive methylation is known to achieve near complete dimethylation of protein amino groups under non-denaturing conditions, in aqueous media. Amino methylation of proteins is employed in mass spectrometric, crystallographic, and NMR studies. Where biosynthetic labeling is prohibitive, amino (13)C-methylation provides an attractive option for monitoring folding, kinetics, protein-protein and protein-DNA interactions by NMR. Here, we… CONTINUE READING