Sandbox Reserved 793 - Revision history

Student at 20:30, 21 October 2013

Student — Mon, 21 Oct 2013 20:30:59 GMT

Student at 21:59, 18 October 2013

Student — Fri, 18 Oct 2013 21:59:29 GMT

←Older revision		Revision as of 21:59, 18 October 2013
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	<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.		<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.
	<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.		<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.
-	<scene name='56/563205/~~Hydrophillic_and_hydrophobic~~/1'>Hydrophilic ~~residues~~</scene> and charged residues(~~dark purple~~) are present in the protein in areas where in it is typically exposed to water.	+	<scene name='56/563205/Hydrophobic_and_philic-_better/1'>Hydrophilic </scene> and charged residues(navy blue) are present in the protein in areas where in it is typically exposed to water.
	==Ligand Interactions==		==Ligand Interactions==
	Several <scene name='56/563205/Interactions/1'>ligand interactions </scene> allow aconitase to form the citrate complex necessary for the citric acid cycle to occur.		Several <scene name='56/563205/Interactions/1'>ligand interactions </scene> allow aconitase to form the citrate complex necessary for the citric acid cycle to occur.
	Looking at these <scene name='56/563205/Interactions_close_up/1'>interactions close up</scene> it is easier to see the different components: the iron-sulfate complex (red and yellow), citrate anion (orange), and oxygen atom (blue).		Looking at these <scene name='56/563205/Interactions_close_up/1'>interactions close up</scene> it is easier to see the different components: the iron-sulfate complex (red and yellow), citrate anion (orange), and oxygen atom (blue).
	The <scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene> (dark green) allow the enzyme to properly bind the ligand and perform the function.		The <scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene> (dark green) allow the enzyme to properly bind the ligand and perform the function.

Student at 21:46, 18 October 2013

Student — Fri, 18 Oct 2013 21:46:15 GMT

←Older revision		Revision as of 21:46, 18 October 2013
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	<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.		<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.
	==Ligand Interactions==		==Ligand Interactions==
-	<scene name='56/563205/Interactions/1'>ligand interactions </scene>	+	Several <scene name='56/563205/Interactions/1'>ligand interactions </scene> allow aconitase to form the citrate complex necessary for the citric acid cycle to occur.
-	<scene name='56/563205/Interactions_close_up/1'>interactions close up</scene>	+	Looking at these <scene name='56/563205/Interactions_close_up/1'>interactions close up</scene> it is easier to see the different components: the iron-sulfate complex (red and yellow), citrate anion (orange), and oxygen atom (blue).
-	<scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene>	+	The <scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene> (dark green) allow the enzyme to properly bind the ligand and perform the function.

Student at 21:35, 18 October 2013

Student — Fri, 18 Oct 2013 21:35:27 GMT

←Older revision		Revision as of 21:35, 18 October 2013
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	==Introduction==		==Introduction==
	The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex.		The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex.
-	The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. ~~THe~~ tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, not quaternary structure is present.	+	==Structural Features==
		+	The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. The tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, not quaternary structure is present.
	<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.		<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.
	<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.		<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.
	<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.		<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.
		+	==Ligand Interactions==
	<scene name='56/563205/Interactions/1'>ligand interactions </scene>		<scene name='56/563205/Interactions/1'>ligand interactions </scene>
	<scene name='56/563205/Interactions_close_up/1'>interactions close up</scene>		<scene name='56/563205/Interactions_close_up/1'>interactions close up</scene>
	<scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene>		<scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene>

Student at 21:34, 18 October 2013

Student — Fri, 18 Oct 2013 21:34:10 GMT

←Older revision		Revision as of 21:34, 18 October 2013
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	<Structure load='1C96' size='500' frame='true' align='right' caption='Aconitase' scene='Insert optional scene name here' />		<Structure load='1C96' size='500' frame='true' align='right' caption='Aconitase' scene='Insert optional scene name here' />
-	==Introduction== The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex.	+	==Introduction==
		+	The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex.
	The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. THe tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, not quaternary structure is present.		The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. THe tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, not quaternary structure is present.
	<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.		<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.

Student at 21:32, 18 October 2013

Student — Fri, 18 Oct 2013 21:32:13 GMT

←Older revision		Revision as of 21:32, 18 October 2013
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	<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.		<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.
	<scene name='56/563205/Interactions/1'>ligand interactions </scene>		<scene name='56/563205/Interactions/1'>ligand interactions </scene>
		+	<scene name='56/563205/Interactions_close_up/1'>interactions close up</scene>
	<scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene>		<scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene>

Student at 21:27, 18 October 2013

Student — Fri, 18 Oct 2013 21:27:17 GMT

←Older revision		Revision as of 21:27, 18 October 2013
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	<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.		<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.
	<scene name='56/563205/Interactions/1'>ligand interactions </scene>		<scene name='56/563205/Interactions/1'>ligand interactions </scene>
-	<scene name='56/563205/~~Catalytic_residues~~/1'>~~catalytic residues~~</scene>	+	<scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene>

Student at 21:06, 18 October 2013

Student — Fri, 18 Oct 2013 21:06:08 GMT

←Older revision		Revision as of 21:06, 18 October 2013
Line 10:		Line 10:
	<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.		<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.
	<scene name='56/563205/Interactions/1'>ligand interactions </scene>		<scene name='56/563205/Interactions/1'>ligand interactions </scene>
		+	<scene name='56/563205/Catalytic_residues/1'>catalytic residues</scene>

Student at 20:55, 18 October 2013

Student — Fri, 18 Oct 2013 20:55:51 GMT

←Older revision		Revision as of 20:55, 18 October 2013
Line 9:		Line 9:
	<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.		<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.
	<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.		<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.
		+	<scene name='56/563205/Interactions/1'>ligand interactions </scene>

Student at 17:36, 18 October 2013

Student — Fri, 18 Oct 2013 17:36:47 GMT

←Older revision		Revision as of 17:36, 18 October 2013
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	<Structure load='1C96' size='500' frame='true' align='right' caption='Aconitase' scene='Insert optional scene name here' />		<Structure load='1C96' size='500' frame='true' align='right' caption='Aconitase' scene='Insert optional scene name here' />
-	==Introduction== The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as ~~the second~~ protein in the citric acid cycle. As a catalyst, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex.	+	==Introduction== The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex.
	The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. THe tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, not quaternary structure is present.		The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. THe tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, not quaternary structure is present.
	<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.		<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.
	<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.		<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.
	<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.		<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.

←Older revision		Revision as of 20:30, 21 October 2013
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	<Structure load='1C96' size='500' frame='true' align='right' caption='Aconitase' scene='Insert optional scene name here' />		<Structure load='1C96' size='500' frame='true' align='right' caption='Aconitase' scene='Insert optional scene name here' />
	==Introduction==		==Introduction==
-	The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex.	+	The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex. This protein can be found both in the cytoplasm and mitochondria of multiple species, but in humans the cystolic form is utilized in the citric acid cycle.
	==Structural Features==		==Structural Features==
-	The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. The tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, ~~not~~ quaternary structure is present.	+	The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. The tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, no quaternary structure is present.
	<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.		<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone.
	<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.		<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein.
-	<scene name='56/563205/Hydrophobic_and_philic-_better/1'>Hydrophilic </scene> and charged residues(navy blue) are present in the protein in areas where in it is typically exposed to water.	+	<scene name='56/563205/Hydrophobic_and_philic-_better/1'>Hydrophilic </scene> and charged residues(navy blue) are present in the protein in areas where it is typically exposed to water.
	==Ligand Interactions==		==Ligand Interactions==
		+	Although its crystallization with water was unable to be shown here, aconitase exists surrounded by water molecules. Water is also able to access the active site of the protein, where it aids in the removal and addition of an OH group from the substrate.
	Several <scene name='56/563205/Interactions/1'>ligand interactions </scene> allow aconitase to form the citrate complex necessary for the citric acid cycle to occur.		Several <scene name='56/563205/Interactions/1'>ligand interactions </scene> allow aconitase to form the citrate complex necessary for the citric acid cycle to occur.
-	Looking at these <scene name='56/563205/Interactions_close_up/1'>interactions close up</scene> it is easier to see the different components: the iron-sulfate complex (~~red~~ and yellow), citrate anion (~~orange~~), and oxygen atom (blue).	+	Looking at these <scene name='56/563205/Interactions_close_up/1'>interactions close up</scene> it is easier to see the different components: the iron-sulfate complex (orange and yellow), citrate anion (red and gray), and oxygen atom (blue). The iron-sulfate complex helps the citrate anion to bind to the active site, which allow the protein to change conformation and form the isocitrate complex of aconitase.
-	The <scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene> (dark green) allow the enzyme to properly bind the ligand and perform the function.	+	The <scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene> (dark green) allow the enzyme to properly bind the ligand and perform the function. Ala642, Asp100, Asp165, Glu262, His101, His147, and His167 are the catalytic groups that allow aconitase to function effectively.