User:Eran Hodis/Sandbox3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Eran Hodis (talk | contribs)
No edit summary
Eran Hodis (talk | contribs)
No edit summary
Line 5: Line 5:
===Introduction===
===Introduction===
The nucleosome core particle contains two copies of each histone protein (H2A, H2B, H3 and H4) and 146 basepairs (bp) of superhelical [[DNA]] wrapped around this histone octamer. It represents the first order of DNA packaging in the nucleus and as such is the principal structure that determines DNA accessibility. The nucleosome core particle contains two copies of each histone protein (H2A, H2B, H3 and H4) and 146 basepairs (bp) of superhelical [[DNA]] wrapped around this histone octamer. It represents the first order of DNA packaging in the nucleus and as such is the principal structure that determines DNA accessibility.  
The nucleosome core particle contains two copies of each histone protein (H2A, H2B, H3 and H4) and 146 basepairs (bp) of superhelical [[DNA]] wrapped around this histone octamer. It represents the first order of DNA packaging in the nucleus and as such is the principal structure that determines DNA accessibility. The nucleosome core particle contains two copies of each histone protein (H2A, H2B, H3 and H4) and 146 basepairs (bp) of superhelical [[DNA]] wrapped around this histone octamer. It represents the first order of DNA packaging in the nucleus and as such is the principal structure that determines DNA accessibility.  
===General Structure===
<h3>General Structure</h3>
There are two distinct classes of HMGRs, class I, which is only found in eukaryotes and are membrane bound and class II, which is found in prokaryotes and are soluble. HMGR contains 8 transmembrane domains that have yet to be successfully crystallized, which anchor the protein to the membrane of the endoplasmic reticulum.
There are two distinct classes of HMGRs, class I, which is only found in eukaryotes and are membrane bound and class II, which is found in prokaryotes and are soluble. HMGR contains 8 transmembrane domains that have yet to be successfully crystallized, which anchor the protein to the membrane of the endoplasmic reticulum.