Proteins & Peptides

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3 (t

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3 (t

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3 (t

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3 (t

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3 (t

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3 (t

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3 (t

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3 (t

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3 (t