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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 ==

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Revision as of 17:45, 17 March 2017

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Contents 1 Zinc Transporter Yiip 2 Structure 3 Helix Orientation 4 Salt Bridge 5 Electrostatic Interactions 6 Conformation Changes 7 References

Zinc Transporter Yiip

Structure

Helix Orientation

Salt Bridge

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 Zn²⁺ 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 Zn²⁺ ions, the C-terminus domains undergo electronegativity alterations, forcing the two domains apart.

Conformation Changes

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</StructureSection>

References