Sandbox Reserved 514 - Revision history

Student at 15:36, 12 May 2012

Student — Sat, 12 May 2012 15:36:57 GMT

←Older revision		Revision as of 15:36, 12 May 2012
Line 1:		Line 1:
-	[[Image:Davids GFP.gif]]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.	+	[[Image:Davids GFP.gif\|thumb\|350px\|left\|trial]]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.

Student at 15:35, 12 May 2012

Student — Sat, 12 May 2012 15:35:08 GMT

←Older revision		Revision as of 15:35, 12 May 2012
Line 1:		Line 1:
-	[[Image:Davids GFP.gif~~.jpg~~]]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.	+	[[Image:Davids GFP.gif]]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.

Student at 15:34, 12 May 2012

Student — Sat, 12 May 2012 15:34:22 GMT

←Older revision		Revision as of 15:34, 12 May 2012
Line 1:		Line 1:
-	Image ~~of PDB entry 1ema from David Goodsell's Molecule of the Month at the RCSB PDB~~.	+	[[Image:Davids GFP.gif.jpg]]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.	+

Student at 15:29, 12 May 2012

Student — Sat, 12 May 2012 15:29:15 GMT

←Older revision		Revision as of 15:29, 12 May 2012
Line 5:		Line 5:
	== Exploring the Structure ==		== Exploring the Structure ==
	<Structure load='1ema' size='300' frame='true' align='right' caption='glow' scene='Insert optional scene name here' />		<Structure load='1ema' size='300' frame='true' align='right' caption='glow' 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/>	+	GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The <scene name='Sandbox_Reserved_514/Gfp-test/2'>chromophore</scene>, 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 14:58:53 GMT

←Older revision		Revision as of 14:58, 12 May 2012
Line 6:		Line 6:
	<Structure load='1ema' size='300' frame='true' align='right' caption='glow' scene='Insert optional scene name here' />		<Structure load='1ema' size='300' frame='true' align='right' caption='glow' 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/>		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 14:58:35 GMT

←Older revision		Revision as of 14:58, 12 May 2012
Line 6:		Line 6:
	<Structure load='1ema' size='300' frame='true' align='right' caption='glow' scene='Insert optional scene name here' />		<Structure load='1ema' size='300' frame='true' align='right' caption='glow' 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/>		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>

Student at 14:55, 12 May 2012

Student — Sat, 12 May 2012 14:55:53 GMT

←Older revision		Revision as of 14:55, 12 May 2012
Line 5:		Line 5:
	== Exploring the Structure ==		== Exploring the Structure ==
	<Structure load='1ema' size='300' frame='true' align='right' caption='glow' scene='Insert optional scene name here' />		<Structure load='1ema' size='300' frame='true' align='right' caption='glow' 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.	+	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/>

Student at 14:52, 12 May 2012

Student — Sat, 12 May 2012 14:52:52 GMT

←Older revision		Revision as of 14:52, 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.
	<Structure load='1ema' size='300' frame='true' align='right' caption='glow' scene='Insert optional scene name here' />		<Structure load='1ema' size='300' frame='true' align='right' caption='glow' 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.

Student at 14:51, 12 May 2012

Student — Sat, 12 May 2012 14:51:05 GMT

←Older revision		Revision as of 14:51, 12 May 2012
Line 2:		Line 2:
	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='300' frame='true' align='right' caption='glow' scene='Insert optional scene name here' />

Student at 14:48, 12 May 2012

Student — Sat, 12 May 2012 14:48:03 GMT

←Older revision		Revision as of 14:48, 12 May 2012
Line 1:		Line 1:
	Image of PDB entry 1ema from David Goodsell's Molecule of the Month at the RCSB PDB.		Image of PDB entry 1ema from David Goodsell's Molecule of the Month at the RCSB PDB.
-	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.