Chemical Modification of Lysine by Reductive Methylation
The basic side chains of lysine residues often play essential roles in DNA-protein recognition. They are able to contribute to the overall affinity of an interaction through nonspecific charge-charge interactions with the phosphate backbone and contribute substantially to the specificity of the interaction by forming direct hydrogen bonds with functional groups on the edges of the bases. This dual role and their almost ubiquitous presence in the interface of DNA-protein complexes make them very attractive targets for chemical modification experiments.
KeywordsFormaldehyde HPLC Urea Acetonitrile Glycine
- 1.Lundblad, R. L. and Noyes, C. M. (1984) Chemical Reagents for Protein Modification. CRC, Boca Raton, FL.Google Scholar
- 9.Thomas, J. O. and Wilson, C. M. (1986) Selective radiolabelling and identification of a strong nucleosome binding site on the globular domain of histone H5. EMBOJ. 5, 3531–3537.Google Scholar