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''Hello''
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[[Image:1ema BIOmics 1.gif]]
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and
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==This is a placeholder==
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welcome to '''Proteopedia'''
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This is a placeholder text to help you get started in
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placing a Jmol applet on your page. At any time, click
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"Show Preview" at the bottom of this page to see how it goes.
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<applet load='1ema' size='300' frame='true' align='right' caption='Insert caption here' />
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== Exploring the Structure ==
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Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
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and display another structure.
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{{STRUCTURE_1ema| PDB=1ema | SCENE= }}
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You can take a close look at the chromophore of '''GFP''' in the PDB entry [[1ema]].
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==My Header==
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[[Image:ericeg.gif|thumb400px|]]
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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.
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The backbone of the entire protein is shown here on the left. The protein chain forms a cylindrical can (shown in blue), with one portion of the strand threading straight through the middle (shown in green). The chromophore is found right in the middle of the can, totally shielded from the surrounding environment. This shielding is essential for the fluorescence. The jostling water molecules would normally rob the chromophore of its energy once it absorbs a photon. But inside the protein, it is protected, releasing the energy instead as a slightly less energetic photon of light. The chromophore (shown in the close-up on the right) forms spontaneously from three amino acids in the protein chain: a glycine, a tyrosine and a threonine (or serine). Notice how the glycine and the threonine have formed a new bond, creating an unusual five-membered ring.
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(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
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{{IPA|}}
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<ref>PMID:8703075</ref>
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==references==
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<reference>
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STRUCTURE_1ema| PDB=1ema | SCENE= }}
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<scene name='Sandbox_7/Chris_1ema/1'>TextToBeDisplayed</scene>
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<scene name='Sandbox_7/Inside/1'>TextT3oBeDisplayed</scene>
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<scene name='Sandbox_7/Chris_1ema/0>Text2ToBeDisplayed</scene>
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{{Reflist}}

Current revision

Image:1ema BIOmics 1.gif

This is a placeholder

This is a placeholder text to help you get started in placing a Jmol applet on your page. At any time, click "Show Preview" at the bottom of this page to see how it goes.

Insert caption here

Drag the structure with the mouse to rotate

Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load and display another structure.


PDB ID 1ema

Drag the structure with the mouse to rotate
1ema, resolution 1.90Å ()
Non-Standard Residues: ,
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



My Header

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.

(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 Template:IPA [1]


references

<reference>


STRUCTURE_1ema| PDB=1ema | SCENE= }}

  1. Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 1996 Sep 6;273(5280):1392-5. PMID:8703075
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