User:Alexander Rudecki/Sandbox 1: Difference between revisions

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The <scene name='58/580851/Composition/1'>composition</scene> of DromeQC consists of either {{Template:ColorKey Composition Protein}}, {{Template:ColorKey Composition Ligand}}, or {{Template:ColorKey Composition Solvent}} in which it was crystallized (water). When DromeQC <scene name='58/580851/Secondary/1'>secondary structure</scene> is colour coated ({{Template:ColorKey_Helix}}, {{Template:ColorKey_Strand}}) the global fold may be visualized nicely. This fold is driven by <scene name='58/580851/Polar/1'>hydrophobic/polar</scene> residues. The majority of {{Template:ColorKey_Hydrophobic}} residues lie in the interior, consistent with the hydrophobic collapse folding theory. Likewise, most {{Template:ColorKey_Polar}} residues reside on the exterior where they contact polar solvent molecules. Similarly, <scene name='58/580851/Charge/1'>charged residues</scene>, either {{Template:ColorKey_Charge_Anionic}} or {{Template:ColorKey_Charge_Cationic}} appear to cluster on the outside of the protein. From these analyses, it can be seen that a salt bridge connects the two monomers.

[[Image:QCtopology.gif|thumb|200px|left|Figure 2. Topology of DromeQC<ref>PDB Sum Entry 4F9U. EMBL-EBI. [https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4f9u&template=protein.html&r=wiring&l=1&chain=A]</ref>]]

Revision as of 20:04, 31 March 2014 view source Alexander Rudecki (talk \| contribs) 167 edits No edit summary ← Older edit		Revision as of 20:05, 31 March 2014 view source Alexander Rudecki (talk \| contribs) 167 edits No edit summary Newer edit →
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	The <scene name='58/580851/Composition/1'>composition</scene> of DromeQC consists of either <span style="font-size:150%">{{Template:ColorKey Composition Protein}}, {{Template:ColorKey Composition Ligand}}</span>, or <span style="font-size:150%">{{Template:ColorKey Composition Solvent}}</span> in which it was crystallized (water). When DromeQC <scene name='58/580851/Secondary/1'>secondary structure</scene> is colour coated <span style="font-size:150%">({{Template:ColorKey_Helix}}, {{Template:ColorKey_Strand}})</span> the global fold may be visualized nicely. This fold is driven by <scene name='58/580851/Polar/1'>hydrophobic/polar</scene> residues. The majority of <span style="font-size:150%">{{Template:ColorKey_Hydrophobic}}</span> residues lie in the interior, consistent with the hydrophobic collapse folding theory. Likewise, most <span style="font-size:150%">{{Template:ColorKey_Polar}}</span> residues reside on the exterior where they contact polar solvent molecules. Similarly, <scene name='58/580851/Charge/1'>charged residues</scene>, either <span style="font-size:150%">{{Template:ColorKey_Charge_Anionic}}</span> or <span style="font-size:150%">{{Template:ColorKey_Charge_Cationic}}</span> appear to cluster on the outside of the protein. From these analyses, it can be seen that a salt bridge connects the two monomers.		The <scene name='58/580851/Composition/1'>composition</scene> of DromeQC consists of either <span style="font-size:150%">{{Template:ColorKey Composition Protein}}, {{Template:ColorKey Composition Ligand}}</span>, or <span style="font-size:150%">{{Template:ColorKey Composition Solvent}}</span> in which it was crystallized (water). When DromeQC <scene name='58/580851/Secondary/1'>secondary structure</scene> is colour coated <span style="font-size:150%">({{Template:ColorKey_Helix}}, {{Template:ColorKey_Strand}})</span> the global fold may be visualized nicely. This fold is driven by <scene name='58/580851/Polar/1'>hydrophobic/polar</scene> residues. The majority of <span style="font-size:150%">{{Template:ColorKey_Hydrophobic}}</span> residues lie in the interior, consistent with the hydrophobic collapse folding theory. Likewise, most <span style="font-size:150%">{{Template:ColorKey_Polar}}</span> residues reside on the exterior where they contact polar solvent molecules. Similarly, <scene name='58/580851/Charge/1'>charged residues</scene>, either <span style="font-size:150%">{{Template:ColorKey_Charge_Anionic}}</span> or <span style="font-size:150%">{{Template:ColorKey_Charge_Cationic}}</span> appear to cluster on the outside of the protein. From these analyses, it can be seen that a salt bridge connects the two monomers.

	[[Image:QCtopology.gif\|thumb\|200px\|left\|Figure 2. Topology of DromeQC<ref>PDB Sum Entry 4F9U. EMBL-EBI. [https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4f9u&template=protein.html&r=wiring&l=1&chain=A]</ref>]]		[[Image:QCtopology.gif\|thumb\|200px\|left\|Figure 2. Topology of DromeQC<ref>PDB Sum Entry 4F9U. EMBL-EBI. [https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4f9u&template=protein.html&r=wiring&l=1&chain=A]</ref>]]