User:Shai Biran/Practice Proteopedia tutorial shai4

Bold and Interwiki

1. In your assigned Sandbox page, now displaying your new text, click “edit this page”.
2. We want to make the word “GFP” bold. Select the word “GFP" and click on the button in the toolbar above the text-editing area with a big “B”.
3. The result should be three single quotation marks on either side of the word “GFP” like so: ’’’GFP’’’
4. Now make “1ema” into an interwiki link, so that it leads to the Proteopedia page for the PDB entry 1ema. Do this by selecting the text “1ema” and clicking on the button in the toolbar above the text-editing area with a big, underlined, blue “Ab”.
5. The result should be two square inward-facing brackets on either side of the word “1ema”. It should look like this: 1ema
6. Save the page using the “Save page” button.

Your page should look like this: ↓↓↓↓↓↓↓↓↓↓↓↓

Your Heading Here (maybe something like 'Structure')

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page Sandbox. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Introduction Green fluorescent protein (GFP), originally isolated from the jellyfish Aequorea victoria (PDB entry 1ema), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement. Exploring the Structure GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The chromophore, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues. This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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Shai Biran