http://52.214.119.220/wiki/index.php?action=history&feed=atom&title=SandboxjgSandboxjg - Revision history2026-04-10T14:13:34ZRevision history for this page on the wikiMediaWiki 1.11.2http://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1324601&oldid=prevJulia Greenberg at 23:01, 25 November 20112011-11-25T23:01:53Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to.</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+<ins style="color: red; font-weight: bold; text-decoration: none;">. [[Image:ClCvideoProteopedia.mov]]</ins>. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td></tr>
</table>Julia Greenberghttp://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1313829&oldid=prevJulia Greenberg at 18:44, 6 November 20112011-11-06T18:44:12Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. [[Image:600px-Fig. 5-1.jpg | <del style="color: red; font-weight: bold; text-decoration: none;">thumb</del>]] In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1'>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1'>(Glu 203)</scene> is involved in H+ permeation.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. [[Image:600px-Fig. 5-1.jpg | <ins style="color: red; font-weight: bold; text-decoration: none;">frame|The three binding sites and the position of Glu 148 in the closed (left) and open (right) positions. </ins>]] In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1'>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1'>(Glu 203)</scene> is involved in H+ permeation.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td></tr>
</table>Julia Greenberghttp://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1313828&oldid=prevJulia Greenberg at 18:34, 6 November 20112011-11-06T18:34:37Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. <del style="color: red; font-weight: bold; text-decoration: none;"> </del>In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1'>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1'>(Glu 203)</scene> is involved in H+ permeation.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. <ins style="color: red; font-weight: bold; text-decoration: none;">[[Image:600px-Fig. 5-1.jpg | thumb]] </ins>In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1'>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1'>(Glu 203)</scene> is involved in H+ permeation.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td></tr>
</table>Julia Greenberghttp://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1304927&oldid=prevJulia Greenberg at 14:13, 29 October 20112011-10-29T14:13:54Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. <del style="color: red; font-weight: bold; text-decoration: none;">[[Image:Fig. 5.jpg]] </del>In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1'>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1'>(Glu 203)</scene> is involved in H+ permeation.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. <ins style="color: red; font-weight: bold; text-decoration: none;"> </ins>In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1'>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1'>(Glu 203)</scene> is involved in H+ permeation.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td></tr>
</table>Julia Greenberghttp://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1304926&oldid=prevJulia Greenberg at 14:04, 29 October 20112011-10-29T14:04:43Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1'>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1'>(Glu 203)</scene> is involved in H+ permeation.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. <ins style="color: red; font-weight: bold; text-decoration: none;">[[Image:Fig. 5.jpg]] </ins>In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1'>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1'>(Glu 203)</scene> is involved in H+ permeation.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td></tr>
</table>Julia Greenberghttp://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1304656&oldid=prevJulia Greenberg at 01:01, 21 October 20112011-10-21T01:01:44Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells , for the transport of electrolytes across epithelial layers, and to.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
</table>Julia Greenberghttp://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1304600&oldid=prevEran Hodis at 16:41, 19 October 20112011-10-19T16:41:38Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/<del style="color: red; font-weight: bold; text-decoration: none;">1’</del>>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/<del style="color: red; font-weight: bold; text-decoration: none;">1’</del>>(Glu 203)</scene> is involved in H+ permeation.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/<ins style="color: red; font-weight: bold; text-decoration: none;">1'</ins>>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/<ins style="color: red; font-weight: bold; text-decoration: none;">1'</ins>>(Glu 203)</scene> is involved in H+ permeation.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td></tr>
</table>Eran Hodishttp://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1304276&oldid=prevHenry Richey at 02:05, 6 October 20112011-10-06T02:05:52Z<p></p>
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<td colspan='2' style="background-color: white; color:black;">Revision as of 02:05, 6 October 2011</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells , for the transport of electrolytes across epithelial layers, and to .</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells , for the transport of electrolytes across epithelial layers, and to.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+.</div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1’>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1’>(Glu 203)</scene> is involved in H+ permeation.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1’>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1’>(Glu 203)</scene> is involved in H+ permeation.</div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td></tr>
</table>Henry Richeyhttp://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1304275&oldid=prevHenry Richey at 02:04, 6 October 20112011-10-06T02:04:30Z<p></p>
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<td colspan='2' style="background-color: white; color:black;">Revision as of 02:04, 6 October 2011</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del style="color: red; font-weight: bold; text-decoration: none;">The </del><scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein <del style="color: red; font-weight: bold; text-decoration: none;">in </del>Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to <del style="color: red; font-weight: bold; text-decoration: none;">regulate cell volume</del>.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein Escherichia coli which belongs to the <ins style="color: red; font-weight: bold; text-decoration: none;"> </ins>CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells , for the transport of electrolytes across epithelial layers, and to .</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+.</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane <ins style="color: red; font-weight: bold; text-decoration: none;">The Cl- and H+ pathways are formed by an extensive network of </ins>interactions <ins style="color: red; font-weight: bold; text-decoration: none;">between the protein and substrates. The Cl- ions are stabilized in </ins>the <ins style="color: red; font-weight: bold; text-decoration: none;">middle </ins>of the <ins style="color: red; font-weight: bold; text-decoration: none;">membrane by the dipole moment of two a</ins>-helices<ins style="color: red; font-weight: bold; text-decoration: none;">, by interactions </ins>with <ins style="color: red; font-weight: bold; text-decoration: none;">amides from the protein’s backbone </ins>and <ins style="color: red; font-weight: bold; text-decoration: none;">by the direct coordination of two conserved side chains</ins>. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane<del style="color: red; font-weight: bold; text-decoration: none;">. Its structure allows it to use electrostatic </del>interactions <del style="color: red; font-weight: bold; text-decoration: none;">with </del>the <del style="color: red; font-weight: bold; text-decoration: none;">dipoles </del>of the <del style="color: red; font-weight: bold; text-decoration: none;">α</del>-helices <del style="color: red; font-weight: bold; text-decoration: none;">and </del>with <del style="color: red; font-weight: bold; text-decoration: none;">nitrogen atoms </del>and <del style="color: red; font-weight: bold; text-decoration: none;">carboxyl groups in order to filter Cl- and H+ ions</del>. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1’>(Glu 148)</scene> functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1’>(Glu 203)</scene> is involved in H+ permeation.</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause <ins style="color: red; font-weight: bold; text-decoration: none;"> </ins>myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>There are 3 chloride binding sites in each monomer, an exterior binding site, a central binding site, and an interior binding site. These three sites span the membrane and define the transport pathway for Cl-. In the structure of the WT protein Glu 148 occupies either the central or the exterior binding sites where it likely competes with Cl- ions. Upon protonation the side chain of E148 extends towards the extracellular solution and opens the pathway allowing ion transport to occur. The H+ transport pathway in each monomer has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1’>(Glu 148)</scene> <del style="color: red; font-weight: bold; text-decoration: none;"> </del>functions as the coupling element between Cl- and H+ while the other <scene name='Sandboxjg/Glu_203/1’>(Glu 203)</scene> is involved in H+ permeation.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>One of the interesting properties of this protein family is that its members can function either as ion channels or transporters. Furthermore, mutating Glu 148 to Ala in CLC-ec1 eliminates H+ transport <del style="color: red; font-weight: bold; text-decoration: none;"> </del>but chloride ions can still move freely through the protein giving rise to a channel-like behavior. Mutations in other family members cause myotonia congenital (CLC-1), osteopetrosis (CLC-7) and kidney pathologies such as Bartter’s syndrome (CLC-Ka and -Kb) and Dent’s disease (CLC-5).</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene></div></td></tr>
</table>Henry Richeyhttp://52.214.119.220/wiki/index.php?title=Sandboxjg&diff=1299944&oldid=prevJulia Greenberg at 00:23, 23 September 20112011-09-23T00:23:04Z<p></p>
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<td colspan='2' style="background-color: white; color:black;">Revision as of 00:23, 23 September 2011</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The <scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein in Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to regulate cell volume.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The <scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein in Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to regulate cell volume.</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+ <del style="color: red; font-weight: bold; text-decoration: none;"> </del>.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane. Its structure allows it to use electrostatic interactions with the dipoles of the α-helices and with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane. Its structure allows it to use electrostatic interactions with the dipoles of the α-helices and with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chain functions independently, we will focus on the structure of one pore.</div></td></tr>
</table>Julia Greenberg