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

Amyloid peptides, derived from amyloid precursor protein (APP), are thought to play a role in the development of the senile plaques associated with Alzheimer’s disease. The amyloid hypothesis presupposes that flaws in the processing of APP result in abnormally high levels of the longer, “stickier” forms of beta amyloid, known as Aβ42 and Aβ43, leading to aggregation of amyloid in the neuronal cell death and ultimately neuronal death. Mutations in the structure of Aβ40 and related peptides as well as in some of the enzymes involved in the processing of APP have been shown to alter the processing of APP. The sporadic (i.e., non-genetic) form of the disease, however, is far more common, caused by aging in concert with a number of both genetic and environmental risk factors.

Amyloid peptides, derived from amyloid precursor protein (APP), are thought to play a role in the development of the senile plaques associated with Alzheimer’s disease. The amyloid hypothesis presupposes that flaws in the processing of APP result in abnormally high levels of the longer, “stickier” forms of beta amyloid, known as Aβ42 and Aβ43, leading to aggregation of amyloid in the neuronal cell death and ultimately neuronal death. Mutations in the structure of Aβ40 and related peptides as well as in some of the enzymes involved in the processing of APP have been shown to alter the processing of APP. The sporadic (i.e., non-genetic) form of the disease, however, is far more common, caused by aging in concert with a number of both genetic and environmental risk factors.

Amyloid peptides, derived from amyloid precursor protein (APP), are thought to play a role in the development of the senile plaques associated with Alzheimer’s disease. The amyloid hypothesis presupposes that flaws in the processing of APP result in abnormally high levels of the longer, “stickier” forms of beta amyloid, known as Aβ42 and Aβ43, leading to aggregation of amyloid in the neuronal cell death and ultimately neuronal death. Mutations in the structure of Aβ40 and related peptides as well as in some of the enzymes involved in the processing of APP have been shown to alter the processing of APP. The sporadic (i.e., non-genetic) form of the disease, however, is far more common, caused by aging in concert with a number of both genetic and environmental risk factors.

Amyloid peptides, derived from amyloid precursor protein (APP), are thought to play a role in the development of the senile plaques associated with Alzheimer’s disease. The amyloid hypothesis presupposes that flaws in the processing of APP result in abnormally high levels of the longer, “stickier” forms of beta amyloid, known as Aβ42 and Aβ43, leading to aggregation of amyloid in the neuronal cell death and ultimately neuronal death. Mutations in the structure of Aβ40 and related peptides as well as in some of the enzymes involved in the processing of APP have been shown to alter the processing of APP. The sporadic (i.e., non-genetic) form of the disease, however, is far more common, caused by aging in concert with a number of both genetic and environmental risk factors.

Amyloid peptides, derived from amyloid precursor protein (APP), are thought to play a role in the development of the senile plaques associated with Alzheimer’s disease. The amyloid hypothesis presupposes that flaws in the processing of APP result in abnormally high levels of the longer, “stickier” forms of beta amyloid, known as Aβ42 and Aβ43, leading to aggregation of amyloid in the neuronal cell death and ultimately neuronal death. Mutations in the structure of Aβ40 and related peptides as well as in some of the enzymes involved in the processing of APP have been shown to alter the processing of APP. The sporadic (i.e., non-genetic) form of the disease, however, is far more common, caused by aging in concert with a number of both genetic and environmental risk factors.

Amyloid peptides, derived from amyloid precursor protein (APP), are thought to play a role in the development of the senile plaques associated with Alzheimer’s disease. The amyloid hypothesis presupposes that flaws in the processing of APP result in abnormally high levels of the longer, “stickier” forms of beta amyloid, known as Aβ42 and Aβ43, leading to aggregation of amyloid in the neuronal cell death and ultimately neuronal death. Mutations in the structure of Aβ40 and related peptides as well as in some of the enzymes involved in the processing of APP have been shown to alter the processing of APP. The sporadic (i.e., non-genetic) form of the disease, however, is far more common, caused by aging in concert with a number of both genetic and environmental risk factors.