User:David Canner/Sandbox good
From Proteopedia
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=====Example from the page [[The Structure of PI3K]] ===== | =====Example from the page [[The Structure of PI3K]] ===== | ||
<center><scene name='User:David_Canner/Sandbox_P/Full/4'>Initial Scene (Reset)</scene> </center> | <center><scene name='User:David_Canner/Sandbox_P/Full/4'>Initial Scene (Reset)</scene> </center> | ||
| - | + | <scene name='User:David_Canner/Sandbox_P/Nsh2_full/1'>The alpha-A helix of NSH2 </scene> (residues 340-345) is anchored into <scene name='User:David_Canner/Sandbox_P/Nsh2_pocket/2'> a cavity created by the C2 and Kinase domain interface.</scene> Helix α11K of the <scene name='User:David_Canner/Sandbox_P/Kinase_domain_out/2'>Kinase domain</scene> (residues 1017-1024) <scene name='User:David_Canner/Sandbox_P/Nsh2_kianse/1'>interacts with the alpha-A helix of nSH2.</scene> nSH2 interacts with the <scene name='User:David_Canner/Sandbox_P/C2_out/3'>C2 domain</scene> through a network of charge-charge interactions involving two loops on nSH2 (Residues 374-377 & 350-354) and C2 residues 364-371, a strong <scene name='User:David_Canner/Sandbox_P/Nsh2_charge_charge/3'>salt bridge between NSH2 Glu 349 and C2 residue Arg 357, and hydrogen bonds between NSH2 Glu 348 and C2 Glu 453 and Asp 454.</scene> | |
| - | + | ====Tip #3: Providing a wide view scene of an area of interest before zooming in provides context==== | |
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| - | <scene name='User:David_Canner/Sandbox_P/Nsh2_full/1'>The alpha-A helix of NSH2 </scene> (residues 340-345) is anchored into <scene name='User:David_Canner/Sandbox_P/Nsh2_pocket/2'> a cavity created by the C2 and Kinase domain interface.</scene> Helix α11K of the <scene name='User:David_Canner/Sandbox_P/Kinase_domain_out/2'>Kinase domain</scene> (residues 1017-1024) <scene name='User:David_Canner/Sandbox_P/Nsh2_kianse/1'>interacts with the alpha-A helix of nSH2.</scene> nSH2 interacts with the <scene name='User:David_Canner/Sandbox_P/C2_out/3'>C2 domain</scene> through a network of charge-charge interactions involving two loops on nSH2 (Residues 374-377 & 350-354) and C2 residues 364-371, a strong <scene name='User:David_Canner/Sandbox_P/Nsh2_charge_charge/3'>salt bridge between NSH2 Glu 349 and C2 residue Arg 357, and hydrogen bonds between NSH2 Glu 348 and C2 Glu 453 and Asp 454.</scene | + | |
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| - | ====Tip # | + | |
=====Example from the page [[The Structure of PI3K]]===== | =====Example from the page [[The Structure of PI3K]]===== | ||
<center><scene name='User:David_Canner/Sandbox_P/Nsh2__and_helical_ligand_out/1'>Initial Scene (Reset)</scene></center> | <center><scene name='User:David_Canner/Sandbox_P/Nsh2__and_helical_ligand_out/1'>Initial Scene (Reset)</scene></center> | ||
This loop in <scene name='User:David_Canner/Sandbox_P/Nsh2__and_helical_ligand_out/2'>the helical domain </scene> which contains the hotspots (residues 542-546) is located precisely where <scene name='User:David_Canner/Sandbox_P/Nsh2_ligand_just_ligand_full/1'> the phosphopeptide of NSH2 ligands, like PDGFR, bind to NSH2.</scene> The salt bridge formed between <scene name='User:David_Canner/Sandbox_P/Nsh2_disruption_of_salt/1'>Glu 542 and nSH2 is disrupted upon binding phosphorylated peptides</scene> like PDGFR, eliminating nSH2-mediated inhibition of p110α and activating the enzyme to phosphorylate PIP2 into PIP3. | This loop in <scene name='User:David_Canner/Sandbox_P/Nsh2__and_helical_ligand_out/2'>the helical domain </scene> which contains the hotspots (residues 542-546) is located precisely where <scene name='User:David_Canner/Sandbox_P/Nsh2_ligand_just_ligand_full/1'> the phosphopeptide of NSH2 ligands, like PDGFR, bind to NSH2.</scene> The salt bridge formed between <scene name='User:David_Canner/Sandbox_P/Nsh2_disruption_of_salt/1'>Glu 542 and nSH2 is disrupted upon binding phosphorylated peptides</scene> like PDGFR, eliminating nSH2-mediated inhibition of p110α and activating the enzyme to phosphorylate PIP2 into PIP3. | ||
| - | + | ====Tip #4: When Transitioning focus to a new domain, it is best to zoom out and orient the reader to the new domain of interest==== | |
| + | =====Example from the page [[The Structure of PI3K]]:===== | ||
| + | <center><scene name='User:David_Canner/Sandbox_P/Full/4'>Initial Scene (Reset)</scene> </center> | ||
| + | <scene name='User:David_Canner/Sandbox_P/Nsh2_full/1'>The alpha-A helix of NSH2 </scene> (residues 340-345) is anchored into <scene name='User:David_Canner/Sandbox_P/Nsh2_pocket/2'> a cavity created by the C2 and Kinase domain interface.</scene> Helix α11K of the <scene name='User:David_Canner/Sandbox_P/Kinase_domain_out/2'>Kinase domain</scene> (residues 1017-1024) <scene name='User:David_Canner/Sandbox_P/Nsh2_kianse/1'>interacts with the alpha-A helix of nSH2.</scene> nSH2 interacts with the <scene name='User:David_Canner/Sandbox_P/C2_out/3'>C2 domain</scene> through a network of charge-charge interactions involving two loops on nSH2 (Residues 374-377 & 350-354) and C2 residues 364-371, a strong <scene name='User:David_Canner/Sandbox_P/Nsh2_charge_charge/3'>salt bridge between NSH2 Glu 349 and C2 residue Arg 357, and hydrogen bonds between NSH2 Glu 348 and C2 Glu 453 and Asp 454.</scene> | ||
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__NOEDITSECTION__ | __NOEDITSECTION__ | ||
__NOTOC__ | __NOTOC__ | ||
Revision as of 10:00, 21 November 2010
How to Make Excellent Scenes
This is a list of tips and tricks to develop effective scenes for your pages. The scenes below were taken from other pages with effective scenes.
Scene Transitions
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