Sandbox Reserved 695: Difference between revisions

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 Structural determination of the VGSC has revealed it to be composed of four homologous domains, each of which has six transmembrane regions, while the pore is composed of the S5 and S6 segments <ref>Sato C, Ueno Y, Asai K, Takahashi K, Sato M, Engel A, Fujiyoshi Y: The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities. Nature 2001, 409:1047-1051.</ref>.  [[Image:VGSC_SCHEMATIC.png]](Image from Wikimedia<ref>http://en.wikipedia.org/wiki/File:Sodium-channel.svg</ref> For a better illustration of the structure, see [http://genomebiology.com/content/figures/gb-2003-4-3-207-1.jpg Schematic of Transmembrane regions of VGSC] <ref>F.H. Yu, W.A. Catterall Overview of the voltage-gated sodium channel superfamily Genome Biol., 4 (2003), pp. 207–214</ref>.)
-For better illustration of the structures at work, the structure shown will only contain one subunit. The <scene name='Sandbox_Reserved_695/Vgsc_alphabeta/2'>secondary structure</scene> includes alpha helices (blue) and beta strands (red). The <scene name='Sandbox_Reserved_695/Vgsc_hydrophobicpolar/2'>hydrophobicity</scene> of the structure reveals that the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Polar}} residues are not exactly easy to illustrate in their membrane bound and subunit bound region.,  but the somewhat diffuse polar regions of the molecule are instrumental in providing the channel with enough hydrophillic residues to allow the passage of ions without allowing significant passage of solvent. In coordination with the hydrophobicity illustration, the <scene name='Sandbox_Reserved_695/Vgsc_evolutionaryconservation/2'>evolutionary conservation</scene> plot shows that both some of the hydrophobic and hydrophillic residues are highly conserved {{Template:ColorKey_ConSurf_NoYellow}}.
+For better illustration of the structures at work, the structure shown will only contain one subunit. The <scene name='Sandbox_Reserved_695/Vgsc_alphabeta/2'>secondary structure</scene> includes <font color='blue'>alpha helices</font> and <font color='red'>beta strands</font>. The <scene name='Sandbox_Reserved_695/Vgsc_hydrophobicpolar/2'>hydrophobicity</scene> of the structure reveals that the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Polar}} residues are not exactly easy to illustrate in their membrane bound and subunit bound region.,  but the somewhat diffuse polar regions of the molecule are instrumental in providing the channel with enough hydrophillic residues to allow the passage of ions without allowing significant passage of solvent. In coordination with the hydrophobicity illustration, the <scene name='Sandbox_Reserved_695/Vgsc_evolutionaryconservation/2'>evolutionary conservation</scene> plot shows that both some of the hydrophobic and hydrophillic residues are highly conserved {{Template:ColorKey_ConSurf_NoYellow}}.
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