Sandbox Reserved 1069: Difference between revisions

[[Image:ElectrostaticV2.png|250px|right|thumb|Figure 1. Electrostatic Charge Distribution]]<scene name='69/694236/Electrostaticv2/1'>Charge Distribution</scene> along the exterior surface of the protein, shown in Figure 1, is primarily neutral (white) for the TMDs, but transitions to positive (blue) near the location of the <scene name='69/694236/Electrostaticv2salt/1'>charge interlock</scene> 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. <scene name='69/694236/Electrostatic_with_zinc/1'>Binding sites</scene> A, B, and C, as well as the CTDs of both monomers, all possess a high negative charge (red) 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 alterations to electronegativity, which enables domain separation.