User:Stephanie Miller/Sandbox32

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has allowed scientists tag cells in order to view them in vivo. The
has allowed scientists tag cells in order to view them in vivo. The
chromophore, which contains the Ser65-Tyr66-Gly67, is stabilized by the
chromophore, which contains the Ser65-Tyr66-Gly67, is stabilized by the
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<scene name='Sandbox/Cfp_bb/1'>beta barrel</scene>that surrounds the structure. Simple modifications to this sequence can allow GFP to undergo several different color
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<scene name='Sandbox/Cfp_bb/1'>beta barrel</scene> that surrounds the structure. Simple modifications to this sequence can allow GFP to undergo several different color
changes. When Tyr66 is changed into W66, the color of GFP changes to <scene name='Sandbox/Cfp1/2'>Cyan Fluorescent Protein (CFP)</scene>. This change allows for the protein to fluoresce blue. The Tyr66 in the GFP molecule plays a primary role in
changes. When Tyr66 is changed into W66, the color of GFP changes to <scene name='Sandbox/Cfp1/2'>Cyan Fluorescent Protein (CFP)</scene>. This change allows for the protein to fluoresce blue. The Tyr66 in the GFP molecule plays a primary role in
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stabilizing the green fluorescent. Whereas GFP contains one tryptophan, CFP contains two tryptophans.
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stabilizing the green fluorescent. Whereas GFP contains one tryptophan, CFP contains two tryptophans.
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This is due to the aromatic rings
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that the amino acid contains. The chromophore in CFP is also stabilized by aromatic rings, however, Likewise, Tryptophan contains aromatic
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rings. In the PDB model 1oxe of CPF, we highlighted the specific amino
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acid that is pertinent in color change from green to blue. The amino
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acid, tryptophan, is colored dark blue in the rasmol model. Along with
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tryptophan, we used a light blue color to display the nitrogen in the
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tryptophan indole ring. A minute change in amino acid Tyr66 allowed for
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the fluorescent protein to go from green to blue. The importance of
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these GFP derivatives is that we are able to trace various types of
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cells at the same time in vitro.
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Revision as of 01:27, 10 March 2009

This page is the sandbox. Use it for making test edits. You may delete everything on this page (but please leave this introductory paragraph).


This is the structure of CFP

Drag the structure with the mouse to rotate

Cyan Fluorescent Protein (CFP)

The protein responsible for the bioluminescence also known as [green fluorescent protein (GFP)] was discovered by scientists in Aequorea victoria. Since then, GFP has revolutionized the field of science and has allowed scientists tag cells in order to view them in vivo. The chromophore, which contains the Ser65-Tyr66-Gly67, is stabilized by the that surrounds the structure. Simple modifications to this sequence can allow GFP to undergo several different color changes. When Tyr66 is changed into W66, the color of GFP changes to . This change allows for the protein to fluoresce blue. The Tyr66 in the GFP molecule plays a primary role in stabilizing the green fluorescent. Whereas GFP contains one tryptophan, CFP contains two tryptophans.

Proteopedia Page Contributors and Editors (what is this?)

Stephanie Miller

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