http://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&feed=atom&action=historyTeam:CIDEB-UANL Mexico/project capture - Revision history2024-03-29T05:25:17ZRevision history for this page on the wikiMediaWiki 1.16.5http://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27796&oldid=prevFernandaPuente at 03:51, 21 June 20142014-06-21T03:51:02Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>This makes an antithesis of theories. Also as it is presented in <b>Figure 5</b>, NhaS is predicted to be exposed and buried, which accords with <b>Figure 6</b>, that show how the amino acids sequence of Nhas is divided many times in exposed and hidden. As nobody has described exactly how is NhaS and where it <del class="diffchange diffchange-inline">would be </del>placed inside <i>E. coli</i>, the team, based on all the modeling above, came out with a hypothesis in which NhaS would cross two times the membrane as it is shown in the <b>Figure 7</b>, having two parts exposed, the beginning loop and the final helix with loop, and an inner part, consisting in the two big helixes as transmembrane and the little loop in the middle of the helixes in the cytoplasmic side. The determinant factor was the structure of NhaS predicted by Raptor X (<b>Figure 4</b>) that is very similar to the transmembrane proteins and ion channels, which are in similar positions, as NhaS in our hypothesis, inside the bacteria.</p><center><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>This makes an antithesis of theories. Also as it is presented in <b>Figure 5</b>, NhaS is predicted to be exposed and buried, which accords with <b>Figure 6</b>, that show how the amino acids sequence of Nhas is divided many times in exposed and hidden. As nobody has described exactly how is NhaS and where it <ins class="diffchange diffchange-inline">is </ins>placed inside <i>E. coli</i>, the team, based on all the modeling above, came out with a hypothesis in which NhaS would cross two times the membrane as it is shown in the <b>Figure 7</b>, having two parts exposed, the beginning loop and the final helix with loop, and an inner part, consisting in the two big helixes as transmembrane and the little loop in the middle of the helixes in the cytoplasmic side. The determinant factor was the structure of NhaS predicted by Raptor X (<b>Figure 4</b>) that is very similar to the transmembrane proteins and ion channels, which are in similar positions, as NhaS in our hypothesis, inside the bacteria.</p><center><br></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p><img width=250 height=200 src="https://static.igem.org/mediawiki/2014hs/1/1b/NhaS_protein_drawing1.jpg"align=center hspace=12 alt="IMG_0317"></p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p><img width=250 height=200 src="https://static.igem.org/mediawiki/2014hs/1/1b/NhaS_protein_drawing1.jpg"align=center hspace=12 alt="IMG_0317"></p></div></td></tr>
</table>FernandaPuentehttp://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27772&oldid=prevFernandaPuente at 03:49, 21 June 20142014-06-21T03:49:01Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p><b>What would happen with Cl- ions?</b></p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p><b>What would happen with Cl<ins class="diffchange diffchange-inline"><SUP></ins>-<ins class="diffchange diffchange-inline"></SUP> </ins>ions?</b></p></div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>After the removal of sodium ions from saltwater, it is needed to remove Cl- ions as well in order to complete the desalination process. E. CARU only captures Na<SUP>+</SUP> ions, leaving Cl- ions in the water medium; but since Cl is a diatomic molecule (meaning it cannot be alone in normal conditions), it joins another Cl molecule, forming Cl<SUB>2</SUB>.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>After the removal of sodium ions from saltwater, it is needed to remove Cl<ins class="diffchange diffchange-inline"><SUP></ins>-<ins class="diffchange diffchange-inline"></SUP> </ins>ions as well in order to complete the desalination process. E. CARU only captures Na<SUP>+</SUP> ions, leaving Cl<ins class="diffchange diffchange-inline"><SUP></ins>-<ins class="diffchange diffchange-inline"></SUP> </ins>ions in the water medium; but since Cl is a diatomic molecule (meaning it cannot be alone in normal conditions), it joins another Cl molecule, forming Cl<SUB>2</SUB>.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Normally, Cl<SUB>2</SUB> is in a gaseous state at normal conditions, so what would remain after E. CARU takes Na<SUP>+</SUP> ions from water is a mixture of Cl<SUB>2</SUB> gas and water molecules. In order to remove it from water it is possible to use a method involving the separation of a gas from a liquid based in the boiling points of each component in the mixture. Cl<SUB>2</SUB> gas has a boiling point of -34.6°C and water has a boiling point of 100°C. By cooling the mixture at -34.6°C, the gas would evaporate, separating itself from water. (Bentor, 2014).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Normally, Cl<SUB>2</SUB> is in a gaseous state at normal conditions, so what would remain after E. CARU takes Na<SUP>+</SUP> ions from water is a mixture of Cl<SUB>2</SUB> gas and water molecules. In order to remove it from water it is possible to use a method involving the separation of a gas from a liquid based in the boiling points of each component in the mixture. Cl<SUB>2</SUB> gas has a boiling point of -34.6°C and water has a boiling point of 100°C. By cooling the mixture at -34.6°C, the gas would evaporate, separating itself from water. (Bentor, 2014).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Yet still, there is an important factor to consider: Cl<SUB>2</SUB> gas is toxic, but as it is 2.5 times heavier than air (CFC StarTec LLC, 2007), it would stay in water at room temperature. For this reason, before cooling the Cl<SUB>2</SUB> gas in order to take it away, it is necessary to take safety measurements. The one proposed by the team is the usage of an Atomic Absorption Spectroscopy (see <b>Figure 2</b>). </p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Yet still, there is an important factor to consider: Cl<SUB>2</SUB> gas is toxic, but as it is 2.5 times heavier than air (CFC StarTec LLC, 2007), it would stay in water at room temperature. For this reason, before cooling the Cl<SUB>2</SUB> gas in order to take it away, it is necessary to take safety measurements. The one proposed by the team is the usage of an Atomic Absorption Spectroscopy (see <b>Figure 2</b>). </p></div></td></tr>
</table>FernandaPuentehttp://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27757&oldid=prevFernandaPuente at 03:47, 21 June 20142014-06-21T03:47:56Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p><b>What would happen with Cl- ions?</b></p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p><b>What would happen with Cl- ions?</b></p></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><p>After the removal of sodium ions from <del class="diffchange diffchange-inline">salty water</del>, it is needed to remove Cl- ions as well in order to complete the desalination process. E. CARU only captures Na<SUP>+</SUP> ions, leaving Cl- ions in the water medium; but since Cl is a diatomic molecule (meaning it cannot be alone in normal conditions), it joins another Cl molecule, forming Cl<SUB>2</SUB>.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>After the removal of sodium ions from <ins class="diffchange diffchange-inline">saltwater</ins>, it is needed to remove Cl- ions as well in order to complete the desalination process. E. CARU only captures Na<SUP>+</SUP> ions, leaving Cl- ions in the water medium; but since Cl is a diatomic molecule (meaning it cannot be alone in normal conditions), it joins another Cl molecule, forming Cl<SUB>2</SUB>.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Normally, Cl<SUB>2</SUB> is in a gaseous state at normal conditions, so what would remain after E. CARU takes Na<SUP>+</SUP> ions from water is a mixture of Cl<SUB>2</SUB> gas and water molecules. In order to remove it from water it is possible to use a method involving the separation of a gas from a liquid based in the boiling points of each component in the mixture. Cl<SUB>2</SUB> gas has a boiling point of -34.6°C and water has a boiling point of 100°C. By cooling the mixture at -34.6°C, the gas would evaporate, separating itself from water. (Bentor, 2014).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Normally, Cl<SUB>2</SUB> is in a gaseous state at normal conditions, so what would remain after E. CARU takes Na<SUP>+</SUP> ions from water is a mixture of Cl<SUB>2</SUB> gas and water molecules. In order to remove it from water it is possible to use a method involving the separation of a gas from a liquid based in the boiling points of each component in the mixture. Cl<SUB>2</SUB> gas has a boiling point of -34.6°C and water has a boiling point of 100°C. By cooling the mixture at -34.6°C, the gas would evaporate, separating itself from water. (Bentor, 2014).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Yet still, there is an important factor to consider: Cl<SUB>2</SUB> gas is toxic, but as it is 2.5 times heavier than air (CFC StarTec LLC, 2007), it would stay in water at room temperature. For this reason, before cooling the Cl<SUB>2</SUB> gas in order to take it away, it is necessary to take safety measurements. The one proposed by the team is the usage of an Atomic Absorption Spectroscopy (see <b>Figure 2</b>). </p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Yet still, there is an important factor to consider: Cl<SUB>2</SUB> gas is toxic, but as it is 2.5 times heavier than air (CFC StarTec LLC, 2007), it would stay in water at room temperature. For this reason, before cooling the Cl<SUB>2</SUB> gas in order to take it away, it is necessary to take safety measurements. The one proposed by the team is the usage of an Atomic Absorption Spectroscopy (see <b>Figure 2</b>). </p></div></td></tr>
</table>FernandaPuentehttp://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27718&oldid=prevOda.ibarra at 03:44, 21 June 20142014-06-21T03:44:25Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>After the removal of sodium ions from salty water, it is needed to remove Cl- ions as well in order to complete the desalination process. E. CARU only captures Na<SUP>+</SUP> ions, leaving Cl- ions in the water medium; but since Cl is a diatomic molecule (meaning it cannot be alone in normal conditions), it joins another Cl molecule, forming Cl<SUB>2</SUB>.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>After the removal of sodium ions from salty water, it is needed to remove Cl- ions as well in order to complete the desalination process. E. CARU only captures Na<SUP>+</SUP> ions, leaving Cl- ions in the water medium; but since Cl is a diatomic molecule (meaning it cannot be alone in normal conditions), it joins another Cl molecule, forming Cl<SUB>2</SUB>.</p></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>Normally, Cl<SUB>2</SUB> is in a gaseous state at normal conditions, so what would remain after E. CARU takes Na+ ions from water is a mixture of Cl<SUB>2</SUB> gas and water molecules. In order to remove it from water it is possible to use a method involving the separation of a gas from a liquid based in the boiling points of each component in the mixture. Cl<SUB>2</SUB> gas has a boiling point of -34.6°C and water has a boiling point of 100°C. By cooling the mixture at -34.6°C, the gas would evaporate, separating itself from water. (Bentor, 2014).</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>Normally, Cl<SUB>2</SUB> is in a gaseous state at normal conditions, so what would remain after E. CARU takes Na<ins class="diffchange diffchange-inline"><SUP></ins>+<ins class="diffchange diffchange-inline"></SUP> </ins>ions from water is a mixture of Cl<SUB>2</SUB> gas and water molecules. In order to remove it from water it is possible to use a method involving the separation of a gas from a liquid based in the boiling points of each component in the mixture. Cl<SUB>2</SUB> gas has a boiling point of -34.6°C and water has a boiling point of 100°C. By cooling the mixture at -34.6°C, the gas would evaporate, separating itself from water. (Bentor, 2014).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Yet still, there is an important factor to consider: Cl<SUB>2</SUB> gas is toxic, but as it is 2.5 times heavier than air (CFC StarTec LLC, 2007), it would stay in water at room temperature. For this reason, before cooling the Cl<SUB>2</SUB> gas in order to take it away, it is necessary to take safety measurements. The one proposed by the team is the usage of an Atomic Absorption Spectroscopy (see <b>Figure 2</b>). </p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Yet still, there is an important factor to consider: Cl<SUB>2</SUB> gas is toxic, but as it is 2.5 times heavier than air (CFC StarTec LLC, 2007), it would stay in water at room temperature. For this reason, before cooling the Cl<SUB>2</SUB> gas in order to take it away, it is necessary to take safety measurements. The one proposed by the team is the usage of an Atomic Absorption Spectroscopy (see <b>Figure 2</b>). </p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Atomic Absorption Spectrometry (AAS) is an analytical technique that measures the concentrations of elements. Atomic absorption is so sensitive that it can measure down to parts per billion of a gram (µg dm–3). The technique uses light wavelengths specifically absorbed by an element that correspond to the energies needed to excite electrons from one energy level to a higher one. (Royal Society of Chemistry).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Atomic Absorption Spectrometry (AAS) is an analytical technique that measures the concentrations of elements. Atomic absorption is so sensitive that it can measure down to parts per billion of a gram (µg dm–3). The technique uses light wavelengths specifically absorbed by an element that correspond to the energies needed to excite electrons from one energy level to a higher one. (Royal Society of Chemistry).</p></div></td></tr>
</table>Oda.ibarrahttp://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27708&oldid=prevOda.ibarra at 03:43, 21 June 20142014-06-21T03:43:19Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p font-size: 8pt><b>Figure 1.</b> Patent US 5346815 A shows extracts of the <i>E. coli</i> EP432 transformed with pGEM <b>(fig. 4A)</b> and pGRVH <b>(fig. 4B)</b>. pGEM is a control plasmid and pGRVH is a plasmid with the nhaS gene. Those are crude extracts shown by the effect of putting the bacteria to an SFBI excitation, which is a sodium-sensitive molecule used to measure intracellular Na+. Resuming, it shows in basic draws that the protein is expressed in <i>E. coli</i> and in what quantity according to the excitation level where it is exposed.</center></p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p font-size: 8pt><b>Figure 1.</b> Patent US 5346815 A shows extracts of the <i>E. coli</i> EP432 transformed with pGEM <b>(fig. 4A)</b> and pGRVH <b>(fig. 4B)</b>. pGEM is a control plasmid and pGRVH is a plasmid with the nhaS gene. Those are crude extracts shown by the effect of putting the bacteria to an SFBI excitation, which is a sodium-sensitive molecule used to measure intracellular Na<ins class="diffchange diffchange-inline"><SUP></ins>+<ins class="diffchange diffchange-inline"></SUP></ins>. Resuming, it shows in basic draws that the protein is expressed in <i>E. coli</i> and in what quantity according to the excitation level where it is exposed.</center></p></div></td></tr>
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</table>Oda.ibarrahttp://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27680&oldid=prevOda.ibarra at 03:40, 21 June 20142014-06-21T03:40:49Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p><b>What would happen with Cl- ions?</b></p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p><b>What would happen with Cl- ions?</b></p></div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>After the removal of sodium ions from salty water, it is needed to remove Cl- ions as well in order to complete the desalination process. E. CARU only captures Na+ ions, leaving Cl- ions in the water medium; but since Cl is a diatomic molecule (meaning it cannot be alone in normal conditions), it joins another Cl molecule, forming Cl<SUB>2</SUB>.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>After the removal of sodium ions from salty water, it is needed to remove Cl- ions as well in order to complete the desalination process. E. CARU only captures Na<ins class="diffchange diffchange-inline"><SUP></ins>+<ins class="diffchange diffchange-inline"></SUP> </ins>ions, leaving Cl- ions in the water medium; but since Cl is a diatomic molecule (meaning it cannot be alone in normal conditions), it joins another Cl molecule, forming Cl<SUB>2</SUB>.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Normally, Cl<SUB>2</SUB> is in a gaseous state at normal conditions, so what would remain after E. CARU takes Na+ ions from water is a mixture of Cl<SUB>2</SUB> gas and water molecules. In order to remove it from water it is possible to use a method involving the separation of a gas from a liquid based in the boiling points of each component in the mixture. Cl<SUB>2</SUB> gas has a boiling point of -34.6°C and water has a boiling point of 100°C. By cooling the mixture at -34.6°C, the gas would evaporate, separating itself from water. (Bentor, 2014).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Normally, Cl<SUB>2</SUB> is in a gaseous state at normal conditions, so what would remain after E. CARU takes Na+ ions from water is a mixture of Cl<SUB>2</SUB> gas and water molecules. In order to remove it from water it is possible to use a method involving the separation of a gas from a liquid based in the boiling points of each component in the mixture. Cl<SUB>2</SUB> gas has a boiling point of -34.6°C and water has a boiling point of 100°C. By cooling the mixture at -34.6°C, the gas would evaporate, separating itself from water. (Bentor, 2014).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Yet still, there is an important factor to consider: Cl<SUB>2</SUB> gas is toxic, but as it is 2.5 times heavier than air (CFC StarTec LLC, 2007), it would stay in water at room temperature. For this reason, before cooling the Cl<SUB>2</SUB> gas in order to take it away, it is necessary to take safety measurements. The one proposed by the team is the usage of an Atomic Absorption Spectroscopy (see <b>Figure 2</b>). </p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Yet still, there is an important factor to consider: Cl<SUB>2</SUB> gas is toxic, but as it is 2.5 times heavier than air (CFC StarTec LLC, 2007), it would stay in water at room temperature. For this reason, before cooling the Cl<SUB>2</SUB> gas in order to take it away, it is necessary to take safety measurements. The one proposed by the team is the usage of an Atomic Absorption Spectroscopy (see <b>Figure 2</b>). </p></div></td></tr>
</table>Oda.ibarrahttp://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27610&oldid=prevOda.ibarra at 03:34, 21 June 20142014-06-21T03:34:49Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>NhaS is a putative protein from <i>Bacillus firmus</i> that is characterized by its ability to bind and sequestering sodium ions, with a calculated weight of 7100 Daltons and a pH of 12. It “can enhance the Na<SUP>+</SUP> -resistance of antiporter- deficient strains by increasing the availability of Na<SUP>+</SUP> to the integral membrane antiporters on the cytoplasmic side of the membrane and by sequestering Na<SUP>+</SUP> while rate-limiting efflux mechanisms catalyze extrusion of the cation.” (Krulwich & Ivey, 1994)</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>NhaS is a putative protein from <i>Bacillus firmus</i> that is characterized by its ability to bind and sequestering sodium ions, with a calculated weight of 7100 Daltons and a pH of 12. It “can enhance the Na<SUP>+</SUP> -resistance of antiporter- deficient strains by increasing the availability of Na<SUP>+</SUP> to the integral membrane antiporters on the cytoplasmic side of the membrane and by sequestering Na<SUP>+</SUP> while rate-limiting efflux mechanisms catalyze extrusion of the cation.” (Krulwich & Ivey, 1994)</p></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><p>Research by Krulwich and Ivey (1994) supports that in its origin bacteria, NhaS works as a <del class="diffchange diffchange-inline">regulation </del>pH <del class="diffchange diffchange-inline">homeostasis </del>protein because it makes the cytoplasmic pH more acidic than the external medium, usually basic.</p> </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>Research by Krulwich and Ivey (1994) supports that in its origin bacteria, NhaS works as a <ins class="diffchange diffchange-inline">regulatory of </ins>pH <ins class="diffchange diffchange-inline">in </ins>protein<ins class="diffchange diffchange-inline">'s homeostasis </ins>because it makes the cytoplasmic pH more acidic than the external medium, usually basic.</p> </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><p>Essentially, NhaS performs three different functions; (1) capturing sodium ions, (2) regulating pH, and (3) enhancing the resistance of bacteria to high saline conditions.</p><center></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Essentially, NhaS performs three different functions; (1) capturing sodium ions, (2) regulating pH, and (3) enhancing the resistance of bacteria to high saline conditions.</p><center></div></td></tr>
</table>Oda.ibarrahttp://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27572&oldid=prevOda.ibarra at 03:31, 21 June 20142014-06-21T03:31:27Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p><b><h2>Description</h2></b></p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p><b><h2>Description</h2></b></p></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><p>NhaS is a putative protein from <i>Bacillus firmus</i> that is characterized by its ability to bind and sequestering sodium ions, with a calculated weight of 7100 Daltons and a pH of 12. It “can enhance the Na+ -resistance of antiporter- deficient strains by increasing the availability of Na+ to the integral membrane antiporters on the cytoplasmic side of the membrane and by sequestering Na+ while rate-limiting efflux mechanisms catalyze extrusion of the cation.” (Krulwich & Ivey, 1994)</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>NhaS is a putative protein from <i>Bacillus firmus</i> that is characterized by its ability to bind and sequestering sodium ions, with a calculated weight of 7100 Daltons and a pH of 12. It “can enhance the Na<ins class="diffchange diffchange-inline"><SUP></ins>+<ins class="diffchange diffchange-inline"></SUP> </ins>-resistance of antiporter- deficient strains by increasing the availability of Na<ins class="diffchange diffchange-inline"><SUP></ins>+<ins class="diffchange diffchange-inline"></SUP> </ins>to the integral membrane antiporters on the cytoplasmic side of the membrane and by sequestering Na<ins class="diffchange diffchange-inline"><SUP></ins>+<ins class="diffchange diffchange-inline"></SUP> </ins>while rate-limiting efflux mechanisms catalyze extrusion of the cation.” (Krulwich & Ivey, 1994)</p></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><p>Research by Krulwich and Ivey (1994) supports that in its origin bacteria, NhaS works as a regulation pH homeostasis protein because it makes the cytoplasmic pH more acidic than the external medium, usually basic.</p> </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Research by Krulwich and Ivey (1994) supports that in its origin bacteria, NhaS works as a regulation pH homeostasis protein because it makes the cytoplasmic pH more acidic than the external medium, usually basic.</p> </div></td></tr>
</table>Oda.ibarrahttp://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27243&oldid=prevFernandaPuente at 03:05, 21 June 20142014-06-21T03:05:58Z<p></p>
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<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><p><del class="diffchange diffchange-inline">Based on the predicted result and with the previous hypothesis the team formulated, it was concluded that the protein would act in the cytoplasmic side of the inner membrane. </del>This <del class="diffchange diffchange-inline">information </del>was used for the understanding and explaining of the module, as well as for designing different animations.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>This <ins class="diffchange diffchange-inline">prediction </ins>was used for the understanding and explaining of the module, as well as for designing different animations.</p></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><p>Further information about NhaS and the experimental results made by the team about it can be found in its <a href="http://parts.igem.org/Part:BBa_K1255000its" target="_blank">parts registry section,</a> as well as the results section in this wiki.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Further information about NhaS and the experimental results made by the team about it can be found in its <a href="http://parts.igem.org/Part:BBa_K1255000its" target="_blank">parts registry section,</a> as well as the results section in this wiki.</p></div></td></tr>
</table>FernandaPuentehttp://2014hs.igem.org/wiki/index.php?title=Team:CIDEB-UANL_Mexico/project_capture&diff=27230&oldid=prevFernandaPuente at 03:04, 21 June 20142014-06-21T03:04:56Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>This makes an antithesis of theories. Also as it is presented in <b>Figure 5</b>, NhaS is predicted to be exposed and buried, which accords with <b>Figure 6</b>, that show how the amino acids sequence of Nhas is divided many times in exposed and hidden. As nobody has described exactly how is NhaS and where it would be placed inside <i>E. coli</i>, the team, based on all the modeling above, came out with a hypothesis in which NhaS would cross two times the membrane as is shown in the <b>Figure 7</b>, having two parts exposed, the beginning loop and the final helix with loop, and an inner part, consisting in the two big helixes as transmembrane and the little loop in the middle of the helixes in the cytoplasmic side. The determinant factor was the structure of NhaS predicted by Raptor X (<b>Figure 4</b>) that is very similar to the transmembrane proteins and ion channels, which are in similar positions, as NhaS in our hypothesis, inside the bacteria.</p><center><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>This makes an antithesis of theories. Also as it is presented in <b>Figure 5</b>, NhaS is predicted to be exposed and buried, which accords with <b>Figure 6</b>, that show how the amino acids sequence of Nhas is divided many times in exposed and hidden. As nobody has described exactly how is NhaS and where it would be placed inside <i>E. coli</i>, the team, based on all the modeling above, came out with a hypothesis in which NhaS would cross two times the membrane as <ins class="diffchange diffchange-inline">it </ins>is shown in the <b>Figure 7</b>, having two parts exposed, the beginning loop and the final helix with loop, and an inner part, consisting in the two big helixes as transmembrane and the little loop in the middle of the helixes in the cytoplasmic side. The determinant factor was the structure of NhaS predicted by Raptor X (<b>Figure 4</b>) that is very similar to the transmembrane proteins and ion channels, which are in similar positions, as NhaS in our hypothesis, inside the bacteria.</p><center><br></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><p><img width=250 height=200 src="https://static.igem.org/mediawiki/2014hs/1/1b/NhaS_protein_drawing1.jpg"align=center hspace=12 alt="IMG_0317"></p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p><img width=250 height=200 src="https://static.igem.org/mediawiki/2014hs/1/1b/NhaS_protein_drawing1.jpg"align=center hspace=12 alt="IMG_0317"></p></div></td></tr>
</table>FernandaPuente