Sandboxjg: Difference between revisions

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The CLC-ec1 (1OTS) protein is a transmembrane

The CLC-ec1 (1OTS) protein is a transmembrane voltage-gated CLC transporter found in Eschrecheria Coli. It is essential to proper electrical activity in muscle cells and some neurons, in the transportion of electrolytes across epithelial layers, and in maintaining proper cell volume.

voltage-gated CLC transporter found in

Eschrecheria Coli. It is essential to proper electrical

activity in muscle cells and some neurons,

in the transportion of electrolytes across

epithelial layers, and in maintaining proper cell

volume~~. Alessio Accardi and his team conducted~~

~~an experiment to learn more about~~

~~the Cl-/H+ exchange that is essential to the~~

~~function of the protein. To assist his team in~~

~~their work, the ECFS SMART Team designed~~

~~a physical model of the protein using Jmol~~.

~~To see~~ the ~~test <scene name='Sandboxjg/Test1ots/~~1~~'>click~~ on ~~me</scene>~~

Roderick MacKinnon and his team determined the structure of the protein and concluded that it was a channel. In a 2004 article co-authored by Accardi and Miller, it was established that the protein functioned by means of a 2:1 chloride ion-hydrogen ion exchange mechanism.

~~<scene name='Sandboxjg/1ots/2'>Hi Hi</scene>~~

The CLC-ec1 transporter is a protein dimer made up of two functional antiparallel polypeptide chains. The chains extend from the inside to the outside of the plasma membrane creating a passage. Its structure allows it to use electrostatic interactions with alpha-helic dipoles and chemical groups coordinated with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chains functions independently, we will focus on the structure of one pore.

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@@ Line 5: / Line 5: @@
 <Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' />
-The CLC-ec1 (1OTS) protein is a transmembrane
+The CLC-ec1 (1OTS) protein is a transmembrane voltage-gated CLC transporter found in Eschrecheria Coli. It is essential to proper electrical activity in muscle cells and some neurons, in the transportion of electrolytes across epithelial layers, and in maintaining proper cell volume.
-voltage-gated CLC transporter found in
-Eschrecheria Coli. It is essential to proper electrical
-activity in muscle cells and some neurons,
-in the transportion of electrolytes across
-epithelial layers, and in maintaining proper cell
-volume. Alessio Accardi and his team conducted
-an experiment to learn more about
-the Cl-/H+ exchange that is essential to the
-function of the protein. To assist his team in
-their work, the ECFS SMART Team designed
-a physical model of the protein using Jmol.
-To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene>
+Roderick MacKinnon and his team determined the structure of the protein and concluded that it was a channel.  In a 2004 article co-authored by  Accardi and Miller, it was established that the protein functioned by means of a 2:1 chloride ion-hydrogen ion exchange mechanism.
-<scene name='Sandboxjg/1ots/2'>Hi Hi</scene>
+The CLC-ec1 transporter is a protein dimer made up of two functional antiparallel polypeptide chains. The chains extend from the inside to the outside of the plasma membrane creating a passage. Its structure allows it to use electrostatic interactions with alpha-helic dipoles and chemical groups coordinated with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chains functions independently, we will focus on the structure of one pore.