Glossy Full Color Sandstone
Nucleosome 3C1B
Made by
Print With Shapeways
Choose Your Size
Choose Your Material
Choose your color and finish
Choose Your Size
$0.00
Choose Your Material
Choose your color and finish
Have a question about this product?
contact the designerYou must be logged in and verified to contact the designer.
Product Description
Model Description
This is a 3D printed model of Nucleosome. The core is made up of 8 histone proteins colored purple according to their bFactor, warmest=pink, coolest=blue. The coiled DNA strand is colored from N to C Terminal blue to red. This allows us to see the anti-parallel winding of one DNA strand to another.
Protein Description
A nucleosome is a structural unit of a eukaryotic chromosome, consisting of a length of DNA coiled around a core of histones.
The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure
Histone methylation regulates chromatin function dependent on the site and degree of the modification. In addition to creating binding sites for proteins, methylated lysine residues are likely to influence chromatin structure directly. Here we present crystal structures of nucleosomes reconstituted with methylated histones and investigate the folding behavior of resulting arrays. We demonstrate that dimethylation of histone H3 at lysine residue 79 locally alters the nucleosomal surface, whereas trimethylation of H4 at lysine residue 20 affects higher-order structure.Created from PDB ID: 3C1B
This is a 3D printed model of Nucleosome. The core is made up of 8 histone proteins colored purple according to their bFactor, warmest=pink, coolest=blue. The coiled DNA strand is colored from N to C Terminal blue to red. This allows us to see the anti-parallel winding of one DNA strand to another.
Protein Description
A nucleosome is a structural unit of a eukaryotic chromosome, consisting of a length of DNA coiled around a core of histones.
The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure
Histone methylation regulates chromatin function dependent on the site and degree of the modification. In addition to creating binding sites for proteins, methylated lysine residues are likely to influence chromatin structure directly. Here we present crystal structures of nucleosomes reconstituted with methylated histones and investigate the folding behavior of resulting arrays. We demonstrate that dimethylation of histone H3 at lysine residue 79 locally alters the nucleosomal surface, whereas trimethylation of H4 at lysine residue 20 affects higher-order structure.Created from PDB ID: 3C1B
Details
What's in the box:
ExSml_nucleosome_3C1B_50
Dimensions:
Success Rate:
First To try.
What's this?
Rating:
Mature audiences only.
