User:Shai Biran/Sandbox 310 - Revision history

Shai Biran: Sandbox 310 moved to User:Shai Biran/Sandbox 310

Shai Biran — Wed, 31 Dec 2014 09:42:30 GMT

Sandbox 310 moved to User:Shai Biran/Sandbox 310

←Older revision

Revision as of 09:42, 31 December 2014

Shai Biran at 11:31, 24 December 2014

Shai Biran — Wed, 24 Dec 2014 11:31:49 GMT

←Older revision		Revision as of 11:31, 24 December 2014
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	== Exploring the Structure ==		== Exploring the Structure ==

-	Eps1 is a Trx-fold protein, with four Trx domains. It is a 75kDa protein made up of 701 amino acids. The <scene name='65/650818/Trx2-cxxc/1'>~~TextToBeDisplayed~~</scene>	+	Eps1 is a Trx-fold protein, with four Trx domains. It is a 75kDa protein made up of 701 amino acids. The <scene name='65/650818/Trx2-cxxc/1'>Trx2-CXXC</scene> is not solvent acceible, unlike any other CXXC motif in other Trx domains.

Shai Biran at 11:30, 24 December 2014

Shai Biran — Wed, 24 Dec 2014 11:30:20 GMT

←Older revision		Revision as of 11:30, 24 December 2014
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	== Exploring the Structure ==		== Exploring the Structure ==

-	Eps1 is a Trx-fold protein, with four Trx domains. It is a 75kDa protein made up of 701 amino acids. The <scene name='61/~~612803~~/~~1ema_chromophore~~/1'>~~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>.	+	Eps1 is a Trx-fold protein, with four Trx domains. It is a 75kDa protein made up of 701 amino acids. The <scene name='65/650818/Trx2-cxxc/1'>TextToBeDisplayed</scene>

Shai Biran at 11:18, 24 December 2014

Shai Biran — Wed, 24 Dec 2014 11:18:34 GMT

←Older revision		Revision as of 11:18, 24 December 2014
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-	==~~Shai's GFP page~~==	+	==Yeast Eps1p==
	<StructureSection load='4TVE' size='340' side='right' caption='GFP' scene=''>		<StructureSection load='4TVE' size='340' side='right' caption='GFP' scene=''>

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	== Introduction ==		== Introduction ==

-	Eps1p, a S. cerevisiae disulfide chaperone, has a part in the ER-associated degradation machinary (PDB entry [[4TVE]]). It is a unique member of the Protein Disulfide Isomerase family of proteins.	+	Eps1p, a ''S. cerevisiae'' disulfide chaperone, has a part in the ER-associated degradation machinary (PDB entry [[4TVE]]). It is a unique member of the Protein Disulfide Isomerase family of proteins.


	== 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 <scene name='61/612803/1ema_chromophore/1'>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>.	+	Eps1 is a Trx-fold protein, with four Trx domains. It is a 75kDa protein made up of 701 amino acids. The <scene name='61/612803/1ema_chromophore/1'>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>.

Shai Biran at 10:34, 24 December 2014

Shai Biran — Wed, 24 Dec 2014 10:34:38 GMT

←Older revision		Revision as of 10:34, 24 December 2014
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	==Shai's GFP page==		==Shai's GFP page==
-	<StructureSection load='~~1ema~~' size='340' side='right' caption='GFP' scene=''>	+	<StructureSection load='4TVE' size='340' side='right' caption='GFP' scene=''>


	== Introduction ==		== 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~~.	+	Eps1p, a S. cerevisiae disulfide chaperone, has a part in the ER-associated degradation machinary (PDB entry [[4TVE]]). It is a unique member of the Protein Disulfide Isomerase family of proteins.
-	~~Exploring the Structure~~	+

Shai Biran at 10:31, 24 December 2014

Shai Biran — Wed, 24 Dec 2014 10:31:05 GMT

←Older revision		Revision as of 10:31, 24 December 2014
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-	==~~Your Heading Here (maybe something like~~ '~~Structure')~~==	+	==Shai's GFP page==
	<StructureSection load='1ema' size='340' side='right' caption='GFP' scene=''>		<StructureSection load='1ema' size='340' side='right' caption='GFP' scene=''>
-	~~This is a default text for your page '''Sandbox 310'''. 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 <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.~~	+

	== Introduction ==		== Introduction ==

Shai Biran at 10:29, 24 December 2014

Shai Biran — Wed, 24 Dec 2014 10:29:15 GMT

←Older revision		Revision as of 10:29, 24 December 2014
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	==Your Heading Here (maybe something like 'Structure')==		==Your Heading Here (maybe something like 'Structure')==
-	<StructureSection load='~~1stp~~' size='340' side='right' caption='~~Caption for this structure~~' scene=''>	+	<StructureSection load='1ema' size='340' side='right' caption='GFP' scene=''>
	This is a default text for your page '''Sandbox 310'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is a default text for your page '''Sandbox 310'''. 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 <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

Shai Biran at 10:20, 24 December 2014

Shai Biran — Wed, 24 Dec 2014 10:20:57 GMT

←Older revision		Revision as of 10:20, 24 December 2014
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	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

-	== ~~introduction~~ ==	+	== 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.		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
		+

	== Exploring the Structure ==		== Exploring the Structure ==

Shai Biran at 10:20, 24 December 2014

Shai Biran — Wed, 24 Dec 2014 10:20:03 GMT

←Older revision		Revision as of 10:20, 24 December 2014
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	This is a default text for your page '''Sandbox 310'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is a default text for your page '''Sandbox 310'''. 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 <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> 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.		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.
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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 <scene name='61/612803/1ema_chromophore/1'>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>.		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='61/612803/1ema_chromophore/1'>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>.

-	== Function ==
-
-	== Disease ==
-
-	== Relevance ==
-
-	== Structural highlights ==

	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.		This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Shai Biran at 10:15, 24 December 2014

Shai Biran — Wed, 24 Dec 2014 10:15:12 GMT

←Older revision		Revision as of 10:15, 24 December 2014
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	This is a default text for your page '''Sandbox 310'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is a default text for your page '''Sandbox 310'''. 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 <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
		+
		+	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 <scene name='61/612803/1ema_chromophore/1'>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>.

	== Function ==		== Function ==