Sandbox 31 - Revision history

Student at 17:02, 26 November 2012

Student — Mon, 26 Nov 2012 17:02:47 GMT

←Older revision		Revision as of 17:02, 26 November 2012
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	<references/>		<references/>
		+
		+	<scene name='Sandbox_31/Rhodopsin_ball_and_chain/1'>Rhodopsin ball and stick</scene>

Hannah Tims — Wed, 05 Sep 2012 01:59:06 GMT

←Older revision		Revision as of 01:59, 5 September 2012
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-	><!-- PLEASE DO NOT DELETE THIS TEMPLATE -->	+	<!-- PLEASE DO NOT DELETE THIS TEMPLATE -->
	{{Template:Oberholser_Sandbox_Reservation}}		{{Template:Oberholser_Sandbox_Reservation}}
	<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->		<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->

Student — Thu, 16 Aug 2012 22:00:21 GMT

←Older revision		Revision as of 22:00, 16 August 2012
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	==Structure==		==Structure==
-	The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). Adenylate kinase has a <scene name='Sandbox_31/Ak_hydrophilic/1'>hydrophilic</scene> exterior, and a <scene name='Sandbox_31/Ak_hydrophobic/1'>hydrophobic</scene> core, with additional	+	The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). A network of <scene name='Sandbox_31/Ak_hydrogen_bonds/1'>hydrogen bonds</scene> hold the secondary structural elements together. You can see the regular hydrogen bonding pattern in the alpha helices.
		+
		+	Adenylate kinase has a <scene name='Sandbox_31/Ak_hydrophilic/1'>hydrophilic</scene> exterior, and a <scene name='Sandbox_31/Ak_hydrophobic/1'>hydrophobic</scene> core, with additional
	<scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand.		<scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand.

Student — Fri, 10 Aug 2012 00:15:34 GMT

←Older revision		Revision as of 00:15, 10 August 2012
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	<scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand.		<scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand.

		+	<scene name='Sandbox_31/Ak_2nd_structure/1'>helix and sheet</scene>
	==Active Site and Mechanism==		==Active Site and Mechanism==

Student — Fri, 10 Aug 2012 00:10:06 GMT

←Older revision		Revision as of 00:10, 10 August 2012
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	Adenylate kinase is caged with <scene name='Sandbox_31/Ak_waters/1'>water molecules</scene>.		Adenylate kinase is caged with <scene name='Sandbox_31/Ak_waters/1'>water molecules</scene>.
		+	==I can add headings==

	This is the <scene name='Sandbox_31/Ak_main/1'>AK</scene> scene.		This is the <scene name='Sandbox_31/Ak_main/1'>AK</scene> scene.

Student — Fri, 10 Aug 2012 00:08:00 GMT

←Older revision		Revision as of 00:08, 10 August 2012
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	Adenylate kinase is caged with <scene name='Sandbox_31/Ak_waters/1'>water molecules</scene>.		Adenylate kinase is caged with <scene name='Sandbox_31/Ak_waters/1'>water molecules</scene>.
-		+
		+	This is the <scene name='Sandbox_31/Ak_main/1'>AK</scene> scene.
		+
	==Structure==		==Structure==
	The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). Adenylate kinase has a <scene name='Sandbox_31/Ak_hydrophilic/1'>hydrophilic</scene> exterior, and a <scene name='Sandbox_31/Ak_hydrophobic/1'>hydrophobic</scene> core, with additional		The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). Adenylate kinase has a <scene name='Sandbox_31/Ak_hydrophilic/1'>hydrophilic</scene> exterior, and a <scene name='Sandbox_31/Ak_hydrophobic/1'>hydrophobic</scene> core, with additional

Student — Wed, 08 Aug 2012 17:00:07 GMT

←Older revision		Revision as of 17:00, 8 August 2012
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	==Structure==		==Structure==
-	The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha ~~helicies~~ (cyan) and beta sheets (green) surrounding the non-~~hydrolyzable~~ substrate analogue (orange). Adenylate kinase has a <scene name='Sandbox_31/Ak_hydrophilic/1'>hydrophilic</scene> exterior, and a <scene name='Sandbox_31/Ak_hydrophobic/1'>hydrophobic</scene> core, with additional	+	The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). Adenylate kinase has a <scene name='Sandbox_31/Ak_hydrophilic/1'>hydrophilic</scene> exterior, and a <scene name='Sandbox_31/Ak_hydrophobic/1'>hydrophobic</scene> core, with additional
	<scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand.		<scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand.

Student — Wed, 08 Aug 2012 14:21:18 GMT

←Older revision		Revision as of 14:21, 8 August 2012
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	together you can see that the <scene name='Sandbox_31/Ak_ligand_binding_and_active_s/1'>active site</scene> is only a fraction of the molecules involved in binding the ligand.		together you can see that the <scene name='Sandbox_31/Ak_ligand_binding_and_active_s/1'>active site</scene> is only a fraction of the molecules involved in binding the ligand.

		+	<Structure load='3be4' size='500' frame='true' align='right' caption='Cryptosporidium parvum' scene='adenylate kinase' />
		+
		+	Comparing the E.coli structure to <scene name='Sandbox_31/Ak_cryptosporidium_parvum/1'>Cryptosporidium parvum</scene>
	==References==		==References==

	<references/>		<references/>

Student — Tue, 07 Aug 2012 18:10:45 GMT

←Older revision		Revision as of 18:10, 7 August 2012
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	adenylate kinase's <scene name='Sandbox_31/Ak_active_site/1'>active site</scene> is highlighted in dark blue.		adenylate kinase's <scene name='Sandbox_31/Ak_active_site/1'>active site</scene> is highlighted in dark blue.

		+	together you can see that the <scene name='Sandbox_31/Ak_ligand_binding_and_active_s/1'>active site</scene> is only a fraction of the molecules involved in binding the ligand.

	==References==		==References==

	<references/>		<references/>

Student — Tue, 07 Aug 2012 18:06:35 GMT

←Older revision		Revision as of 18:06, 7 August 2012
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	residues within <scene name='Sandbox_31/Ak_ligand_binding/3'>3 angstroms</scene> of the ligand are involved in binding the ligand or stabilizing the active site.		residues within <scene name='Sandbox_31/Ak_ligand_binding/3'>3 angstroms</scene> of the ligand are involved in binding the ligand or stabilizing the active site.

-		+	adenylate kinase's <scene name='Sandbox_31/Ak_active_site/1'>active site</scene> is highlighted in dark blue.