Histone H3 (1-20) K4Me2 is derived from Histone 3 (H3), which is one of the four core histones (H2A, H2B, H3 and H4) fundamental in compacting eukaryotic DNA into the nucleosome. The nucleosome arises when 147 base pairs of DNA wrap around a H3-H4 tetramer and two H2A-H2B dimers, forming the histone octamer core. H4 and H3 are highly conserved and perform roles in binding to segments of DNA which enter and leave the nucleosome and in chromatin formation. Like the other core histone, H3 has a globular domain and a flexible N-terminal domain, “histone tail” which can undergo modifications such as acetylation, methylation, phosphorylation and ubiquitination. Due to histones containing many lysine and arginine residues, they have a positive net charge which interacts electrostatically with the negatively charged phosphate groups in DNA. The transcriptional activation or silencing of the chromatin is controlled by ATP-dependent chromatin remodelling factors and histone-modifying enzymes which target histone proteins. Both processes change the positioning of the nucleosome, allowing the DNA to be either available to the transcription machinery or inaccessible.

Histone tails can undergo multiple modifications, including acetylation, methylation, ubiquitylation and sumoylation.  The modification pattern is believed to alter chromatin function/structure. Histone H3 (1-20) K4Me2-GG-[Lys(5-FAM)] lysine 4 has been dimethylated, has a C-terminal GGK linker labelled with 5-Carboxyfluorescein (5-FAM), a widely used green fluorescent tag. This peptide also has an uncharged C-terminal amide. H3 (1-20) K4Me2 has been investigated to understand its effect on epigenetic regulation through NMR with histone readers such as zinc finger domains. Histone H3 (1-20) K4Me2-GG-[Lys(5-FAM)] can be used to study the function of this pattern on chromatin availability and histone effectors via crystallisation, pull-down assays and protein blots.