User:David Canner/Sandbox good: Difference between revisions
David Canner (talk | contribs) No edit summary |
David Canner (talk | contribs) No edit summary |
||
| Line 6: | Line 6: | ||
==Scene Transitions== | ==Scene Transitions== | ||
===Smooth Transitions=== | ===Smooth Transitions=== | ||
<StructureSection load='1dq8' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])'> | <StructureSection load='1dq8' size='500' side='right' scene='HMG-CoA_Reductase/1dq8_starting_scene/1' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])'> | ||
Example from the page [[HMG-CoA Reductase]]: | Example from the page [[HMG-CoA Reductase]]: | ||
Revision as of 11:34, 21 November 2010
How to make excellent scenes:
This is a list of tips and tricks to develop effective scenes for your pages.
Tip #1: When developing a series of scenes illustrating related parts of a protein, use the “transition options” to create smooth transitions void of peculiar zoom-outs, etc.
Scene TransitionsScene Transitions
Smooth TransitionsSmooth Transitions
Example 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… |
| ||||||||||