Sandbox 44 - Revision history

Student: /* Structure */

Student — Fri, 19 Oct 2012 17:38:22 GMT

Structure

←Older revision		Revision as of 17:38, 19 October 2012
Line 8:		Line 8:
	The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).		The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).
	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> (blue)that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues (purple) located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.		The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> (blue)that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues (purple) located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.
-	The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.	+	The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> (orange) in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> (yellow) that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> (maroon) can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.

	=Sources=		=Sources=
	http://en.wikipedia.org/wiki/Adenylate_kinase		http://en.wikipedia.org/wiki/Adenylate_kinase
	http://www.proteopedia.org/wiki/index.php/Adenylate_kinase		http://www.proteopedia.org/wiki/index.php/Adenylate_kinase

Student: /* Structure */

Student — Fri, 19 Oct 2012 17:37:09 GMT

Structure

←Older revision		Revision as of 17:37, 19 October 2012
Line 7:		Line 7:
	The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices.		The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices.
	The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).		The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).
-	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> (blue)that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.	+	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> (blue)that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues (purple) located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.
	The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.		The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.

Student: /* Structure */

Student — Fri, 19 Oct 2012 17:36:26 GMT

Structure

←Older revision		Revision as of 17:36, 19 October 2012
Line 7:		Line 7:
	The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices.		The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices.
	The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).		The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).
-	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.	+	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> (blue)that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.
	The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.		The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.

Student at 17:31, 19 October 2012

Student — Fri, 19 Oct 2012 17:31:52 GMT

←Older revision		Revision as of 17:31, 19 October 2012
Line 9:		Line 9:
	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.		The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.
	The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.		The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.
		+
		+	=Sources=
		+	http://en.wikipedia.org/wiki/Adenylate_kinase
		+	http://www.proteopedia.org/wiki/index.php/Adenylate_kinase

Student at 17:28, 19 October 2012

Student — Fri, 19 Oct 2012 17:28:41 GMT

←Older revision		Revision as of 17:28, 19 October 2012
Line 9:		Line 9:
	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.		The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.
	The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.		The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.
-
-	<scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene>
-
-
-	<scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene>

Student at 17:28, 19 October 2012

Student — Fri, 19 Oct 2012 17:28:06 GMT

←Older revision		Revision as of 17:28, 19 October 2012
Line 7:		Line 7:
	The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices.		The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices.
	The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).		The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).
-	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.	+	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.
		+	The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.

-	~~<scene name='Sandbox_44/Solvent/1'>solvent</scene>~~	+	<scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene>
-		+
-	<scene name='Sandbox_44/Ligand_interraction/1'>ligand ~~interraction~~</scene>	+


	<scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene>		<scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene>

Student at 17:17, 19 October 2012

Student — Fri, 19 Oct 2012 17:17:04 GMT

←Older revision		Revision as of 17:17, 19 October 2012
Line 5:		Line 5:
	Adenylate Kinase is an enzyme that helps in the conversion of 2 units of ADP into one of ATP and one of AMP. It has two chains:<Structure load='1AKE A' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='' /> <scene name='Sandbox_44/Chain_a/3'>Chain A</scene> and Chain B. Adenylate Kinase plays an important role in cell energy homeostatis because of of its function. It is made of 214 amino acids.		Adenylate Kinase is an enzyme that helps in the conversion of 2 units of ADP into one of ATP and one of AMP. It has two chains:<Structure load='1AKE A' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='' /> <scene name='Sandbox_44/Chain_a/3'>Chain A</scene> and Chain B. Adenylate Kinase plays an important role in cell energy homeostatis because of of its function. It is made of 214 amino acids.
	=Structure=		=Structure=
-		+	The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices.
-	The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).	+	The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).
	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.		The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.

Student at 17:15, 19 October 2012

Student — Fri, 19 Oct 2012 17:15:48 GMT

←Older revision		Revision as of 17:15, 19 October 2012
Line 6:		Line 6:
	=Structure=		=Structure=

-	The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up). The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.	+	The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up).
		+	The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.

	<scene name='Sandbox_44/Solvent/1'>solvent</scene>		<scene name='Sandbox_44/Solvent/1'>solvent</scene>

Student at 17:14, 19 October 2012

Student — Fri, 19 Oct 2012 17:14:56 GMT

←Older revision		Revision as of 17:14, 19 October 2012
Line 5:		Line 5:
	Adenylate Kinase is an enzyme that helps in the conversion of 2 units of ADP into one of ATP and one of AMP. It has two chains:<Structure load='1AKE A' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='' /> <scene name='Sandbox_44/Chain_a/3'>Chain A</scene> and Chain B. Adenylate Kinase plays an important role in cell energy homeostatis because of of its function. It is made of 214 amino acids.		Adenylate Kinase is an enzyme that helps in the conversion of 2 units of ADP into one of ATP and one of AMP. It has two chains:<Structure load='1AKE A' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='' /> <scene name='Sandbox_44/Chain_a/3'>Chain A</scene> and Chain B. Adenylate Kinase plays an important role in cell energy homeostatis because of of its function. It is made of 214 amino acids.
	=Structure=		=Structure=
		+
	The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up). The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.		The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up). The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.
		+
	<scene name='Sandbox_44/Solvent/1'>solvent</scene>		<scene name='Sandbox_44/Solvent/1'>solvent</scene>

Student at 17:14, 19 October 2012

Student — Fri, 19 Oct 2012 17:14:14 GMT

←Older revision		Revision as of 17:14, 19 October 2012
Line 3:		Line 3:
	<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->		<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
	=Adenylate Kinase=		=Adenylate Kinase=
-	Adenylate Kinase is an enzyme that helps in the conversion of 2 units of ADP into one of ATP and one of AMP. It has two chains:<Structure load='1AKE A' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='' /> <scene name='Sandbox_44/Chain_a/3'>Chain A</scene> and Chain B. Adenylate Kinase plays an important role in cell energy homeostatis because of of its function.	+	Adenylate Kinase is an enzyme that helps in the conversion of 2 units of ADP into one of ATP and one of AMP. It has two chains:<Structure load='1AKE A' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='' /> <scene name='Sandbox_44/Chain_a/3'>Chain A</scene> and Chain B. Adenylate Kinase plays an important role in cell energy homeostatis because of of its function. It is made of 214 amino acids.
-	<scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> ~~The~~ alpha helices ~~are~~ purple and the beta sheets ~~are~~ lime green. <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> ~~The hydrogen bonds~~ of the backbone are shown in yellow. ~~YOU NEED TO TALK ABOUT BETA SHEETS~~.	+	=Structure=
-	<scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene>	+	The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up). The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site.
-		+
-	<scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene>	+
-		+
-	~~<scene name='Sandbox_47/Adenylate_kinase_hydrophillic/1'>Polar Residues</scene>~~	+
-		+
	<scene name='Sandbox_44/Solvent/1'>solvent</scene>		<scene name='Sandbox_44/Solvent/1'>solvent</scene>