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While solution state NMR is very well suited for analysis of protein-protein interactions occurring with a wide range of affinities, it suffers from one significant weakness, known as the molecular weight limitation. This limitation stems from the efficient nuclear relaxation processes in macromolecules larger than 30 kDa (Wider & Wuthrich, 1999). These relaxation processes cause rapid decay of NMR signals. Although the use of transverse relaxation optimized spectroscopy (TROSY) approaches has made solution state NMR of large proteins and protein-protein complexes more feasible, it is still limited by the ability to produce isotope enriched proteins (Pervushin et al., 1997). However, there is a significant number of proteins for which no convenient system for stable isotope incorporation exists. We recently utilized reductive methylation methodology to demonstrate that it is possible to introduce 13C-enriched methyl groups into lysine residues in otherwise unlabeled proteins with the purpose of studying protein-ligand and protein-protein interactions by NMR (Abraham et al., 2008).

The Use of Reductive Methylation of Lysine Residues to Study Protein-Protein Interactions in High Molecular Weight Complexes by Solution NMR