Sandbox Reserved 515 - Revision history

Student at 14:59, 12 May 2012

Student — Sat, 12 May 2012 14:59:07 GMT

←Older revision		Revision as of 14:59, 12 May 2012
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-	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.	+	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 ==		== 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.
-	ref.PMID: 8703075 </ref>
	<Structure load='1ema' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here'/>		<Structure load='1ema' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here'/>
		+
		+	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.
		+	<ref>PMID: 8703075 </ref>

	<references/>		<references/>

Student at 14:58, 12 May 2012

Student — Sat, 12 May 2012 14:58:17 GMT

←Older revision		Revision as of 14:58, 12 May 2012
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	== Exploring the Structure ==		== 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.		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.
-	ref.PMID: 8703075 <~~ref~~/>	+	ref.PMID: 8703075 </ref>
-	<Structure load='1ema' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />	+	<Structure load='1ema' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here'/>

	<references/>		<references/>

Student at 14:57, 12 May 2012

Student — Sat, 12 May 2012 14:57:29 GMT

←Older revision		Revision as of 14:57, 12 May 2012
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	== Exploring the Structure ==		== 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.		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.
-	ref.PMID: 8703075 <ref/	+	ref.PMID: 8703075 <ref/>
	<Structure load='1ema' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />		<Structure load='1ema' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
		+
		+	<references/>

Student at 14:55, 12 May 2012

Student — Sat, 12 May 2012 14:55:54 GMT

←Older revision		Revision as of 14:55, 12 May 2012
Line 4:		Line 4:
	== Exploring the Structure ==		== 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.		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.
		+	ref.PMID: 8703075 <ref/
	<Structure load='1ema' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />		<Structure load='1ema' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Student at 14:51, 12 May 2012

Student — Sat, 12 May 2012 14:51:55 GMT

←Older revision		Revision as of 14:51, 12 May 2012
Line 4:		Line 4:
	== Exploring the Structure ==		== 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.		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.
-	<Structure load='1ema' size='~~500~~' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />	+	<Structure load='1ema' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Student at 14:51, 12 May 2012

Student — Sat, 12 May 2012 14:51:35 GMT

←Older revision		Revision as of 14:51, 12 May 2012
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	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.		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	+
		+	== 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.		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.
		+	<Structure load='1ema' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

Student at 14:48, 12 May 2012

Student — Sat, 12 May 2012 14:48:02 GMT

←Older revision		Revision as of 14:48, 12 May 2012
Line 1:		Line 1:
-	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.	+	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		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.		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.

Student at 14:45, 12 May 2012

Student — Sat, 12 May 2012 14:45:23 GMT

←Older revision	Revision as of 14:45, 12 May 2012
Line 1:	Line 1:
	+	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.

Student: Removing all content from page

Student — Sat, 12 May 2012 14:41:33 GMT

Removing all content from page

←Older revision		Revision as of 14:41, 12 May 2012
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David Canner — Sun, 06 May 2012 19:29:10 GMT

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