Sandbox Reserved 1771: Difference between revisions

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===Transmembrane Interactions===

Many transmembrane interactions can be found within a IgM B-cell receptor. The <scene name='95/952699/Transmembrane_region/1'>α and β subunits</scene> have numerous interactions that keep them associated with each other. An overview of all residue interactions can be found <scene name='95/952699/Overview_hbonds_fixed/2'>here</scene> (highlighted in green). At a cellular pH, various amino acid residues found in the transmembrane region are charged as well, which strengthens the overall interaction. For example, <scene name='95/952699/N155_e138_hbonds_fixed/2'>a hydrogen bond</scene> between residues N155 and E138, along with numerous other hydrogen bonds, works to stabilize the α-β chain interactions. Further down the chains, <scene name='95/952699/T166_e148_hbonds_fixed/2'>interactions</scene> between residues T166 and E148 also have strong hydrogen bonding. Overall, these hydrogen bonds and ion interactions work to maintain the association of the α-β chains.

Many transmembrane interactions can be found within a IgM B-cell receptor. The <scene name='95/952699/Transmembrane_region/1'>α and β subunits</scene> have numerous interactions that keep them associated with each other. An overview of all residue interactions can be found <scene name='95/952699/Overview_hbonds_fixed/2'>here</scene> (highlighted in green). At a cellular pH, various amino acid residues found in the transmembrane region are charged as well, which strengthens the overall interaction. For example, <scene name='95/952699/N155_e138_hbonds_fixed/2'>a hydrogen bond</scene> between residues N155 and E138, along with numerous other hydrogen bonds, works to stabilize the α-β chain interactions. Further down the chains, <scene name='95/952699/T166_e148_hbonds_fixed/3'>interactions</scene> between residues T166 and E148 also have strong hydrogen bonding. Overall, these hydrogen bonds and ion interactions work to maintain the association of the α-β chains.

</StructureSection>

Sandbox Reserved 1771: Difference between revisions

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@@ Line 17: / Line 17: @@
 ===Transmembrane Interactions===
-Many transmembrane interactions can be found within a IgM B-cell receptor. The <scene name='95/952699/Transmembrane_region/1'>α and β subunits</scene> have numerous interactions that keep them associated with each other. An overview of all residue interactions can be found <scene name='95/952699/Overview_hbonds_fixed/2'>here</scene> (highlighted in green). At a cellular pH, various amino acid residues found in the transmembrane region are charged as well, which strengthens the overall interaction. For example, <scene name='95/952699/N155_e138_hbonds_fixed/2'>a hydrogen bond</scene> between residues N155 and E138, along with numerous other hydrogen bonds, works to stabilize the α-β chain interactions. Further down the chains, <scene name='95/952699/T166_e148_hbonds_fixed/2'>interactions</scene> between residues T166 and E148 also have strong hydrogen bonding. Overall, these hydrogen bonds and ion interactions work to maintain the association of the α-β chains.
+Many transmembrane interactions can be found within a IgM B-cell receptor. The <scene name='95/952699/Transmembrane_region/1'>α and β subunits</scene> have numerous interactions that keep them associated with each other. An overview of all residue interactions can be found <scene name='95/952699/Overview_hbonds_fixed/2'>here</scene> (highlighted in green). At a cellular pH, various amino acid residues found in the transmembrane region are charged as well, which strengthens the overall interaction. For example, <scene name='95/952699/N155_e138_hbonds_fixed/2'>a hydrogen bond</scene> between residues N155 and E138, along with numerous other hydrogen bonds, works to stabilize the α-β chain interactions. Further down the chains, <scene name='95/952699/T166_e148_hbonds_fixed/3'>interactions</scene> between residues T166 and E148 also have strong hydrogen bonding. Overall, these hydrogen bonds and ion interactions work to maintain the association of the α-β chains.
 </StructureSection>