Sandbox Reserved 1067: Difference between revisions
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== Electrostatic Interactions == | == Electrostatic Interactions == | ||
Charge distribution along the exterior surface of the protein is primarily neutral for the trans-membrane domains, 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. Binding sites A, B, and C, as well as the C-terminus domains of both monomers, all possess a high negative charge relative to the other charges present, facilitating the binding and releasing of Zn<sup>2+</sup> ions. The two C-terminus domains are held together by the charge interlock and hydrophobic interactions of the trans-membrane domains despite their electrostatic repulsion. Upon the release of Zn<sup>2+</sup> ions, the C-terminus domains undergo electronegativity alterations, forcing the two domains apart. | |||
== Conformation Changes == | == Conformation Changes == | ||
