Review of Methods to Assign the NMR Peaks of Reductively Methylated Proteins
 

Review of Methods to Assign the NMR Peaks of Reductively Methylated Proteins

Publication date: Available online 28 August 2014
Source:Analytical Biochemistry</br>
Author(s): Kevin J. Roberson , Megan A. Macnaughtan</br>
Reductive methylation of lysyl side-chain amines has been a successful tool in the advancement of high resolution structural biology. The utility of this method has continuously gained ground as a protein chemical modification; first, as a tool to aid protein crystallization and later, as a probe in protein nuclear magnetic resonance (NMR) spectroscopy. As an isotope-labeling strategy for NMR studies, reductive methylation has contributed to the study of protein-protein interactions and global conformational changes. While more detailed structural studies using this labeling strategy are possible, the hurdle of assigning the NMR peaks to the corresponding reductively methylated amine hinders its use. In this review, we discuss and compare strategies used to assign the NMR peaks of reductively methylated protein-amines.
</br></br>
</br></br>

More...