Sandbox Reserved 1067: Difference between revisions

[[Image:Yiip_Electrostatic.png|250px|left|thumb|Electrostatics]]<scene name='69/694234/Electro/1'>Charge distribution</scene> along the exterior surface of the protein is primarily neutral for the TMDs, but transitions to positive near the location of the charge interlock and interior side of the cell membrane. This positive section is characteristic of trans-membrane proteins as a means of achieving proper orientation within the cell membrane. Binding sites A, B, and C, as well as the CTDs of both monomers, all possess a high negative charge relative to the other charges present, facilitating the binding and releasing of Zn²⁺ ions. The two CTDs are held together by the charge interlock and hydrophobic interactions of the TMDs despite their electrostatic repulsion. Upon the release of Zn²⁺ ions, the CTDs undergo electronegativity alterations that enable domain separation.