Compared with differentiated somatic cells, ESCs have unique features: they have a more "open" conformation of chromatin structure, including the telomeric region.
Structural modeling in the absence of calcium suggests that mini-calpain-5 adopts a more open conformation when compared to previously determined structures of other calpain cores.
Polymerization also produced deuteration increases for peptide fragments containing the ATP phosphate-binding loops, suggesting G-actin transitions to a more "open" conformation upon polymerization.
In the absence of cAMP, this region moves slightly away from the PBC resulting in a more open conformation.
These data support a model in which SM proteins hold their cognate syntaxins in a closed conformation and thus regulate SNARE complex assembly, perhaps by facilitating the switch of syntaxins from their closed to a more open conformation [7].
Since a conformational change from a closed to a more open structure is likely the rate-determining step in the IDE reaction, the subunit induced conformational change likely shifts the structure of the oligomeric enzyme to a more open conformation.
On a cytological level, functionally different types of chromatin have been described: euchromatin appears less condensed, is thought to have a more "open" conformation, contains the majority of genes, replicates early and throughout S-phase, and is mostly transcriptionally active.
