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. | <scene name='69/694234/Electrostatic/1'>Charge distribution</scene> 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 == | ||
Revision as of 18:31, 17 March 2017
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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
This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
