User:David Canner/Sandbox good: Difference between revisions
David Canner (talk | contribs) No edit summary |
David Canner (talk | contribs) No edit summary |
||
| Line 24: | Line 24: | ||
====Tip #4: Providing a wide view scene of an area of interest before zooming in provides context==== | ====Tip #4: Providing a wide view scene of an area of interest before zooming in provides context==== | ||
=====Example from the page [[The Structure of PI3K]]===== | =====Example from the page [[The Structure of PI3K]]===== | ||
<center><scene name=' | <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. | ||
Revision as of 12:40, 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
Smooth TransitionsExample from the page HMG-CoA Reductase:The HMG binding pocket is the site of catalysis in HMGR. is a critical structural element of this binding site. Residues and are positioned in the active site as is . It is this K691 that likely stabilizes the negatively charged oxygen of the first mevaldyl-CoA intermediate. The mevaldyl CoA intermediate is subsequently converted to Mavaldehyde with added stabilization from . It is then believed that the close proximity of increases the pKA of E559, allowing it to be a proton donor for the reduction of mevaldehyde into mevalonate. Compared with:The HMG binding pocket is the site of catalysis in HMGR. is a critical structural element of this binding site. Residues and are positioned in the active site as is . Etc… Tip #2: It is best to establish a color scheme for all domains of interest and to stick with this color scheme throughout the analysisExample from the page The Structure of PI3KCompared with:Tip #3: When Transitioning focus to a new domain, it is best to zoom out and orient the reader to the new domain of interestExample from the page The Structure of PI3K:(residues 340-345) is anchored into Helix α11K of the (residues 1017-1024) nSH2 interacts with the through a network of charge-charge interactions involving two loops on nSH2 (Residues 374-377 & 350-354) and C2 residues 364-371, a strong [1]
Tip #4: Providing a wide view scene of an area of interest before zooming in provides contextExample from the page The Structure of PI3KThis loop in which contains the hotspots (residues 542-546) is located precisely where The salt bridge formed between like PDGFR, eliminating nSH2-mediated inhibition of p110α and activating the enzyme to phosphorylate PIP2 into PIP3.
|
| ||||||||||