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-	{{Template: Oberholser Sandbox Reservation}}	+	<!-- PLEASE DO NOT DELETE THIS TEMPLATE -->
-	<applet load='1QLQ' size='300' frame='true' align='right' caption='Bovine Pancreatic Trypsin' />	+	{{Template:Oberholser_Sandbox_Reservation}}
		+	<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
		+	=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. It is made of 214 amino acids.
		+	=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> (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> (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.
-	=Trypsin=	+	=Sources=
-		+	http://en.wikipedia.org/wiki/Adenylate_kinase
-	Trypsin is a serine protease that is produced in the pancreas. Serine protease means that it is an enzyme that cleaves amino acid sequences and that a serine residue is located in the active site of the enzyme. In order to prevent it from breaking down the proteins in the pancreas of the organism that produces it, it is first produced as the inactive zymogen, proenzyme trypsinogen.	+	http://www.proteopedia.org/wiki/index.php/Adenylate_kinase
-		+
-	==Structural Aspects==	+
-		+
-	Trypsin is an enzyme that is composed of one, sequence unique, chain consisting of 58 amino acid residues. Looking at the <scene name='Sandbox_44/Secondary_structure_of_trypsin/1'>Secondary Structure</scene> of trypsin one can see it is composed of two alpha helices(pink) and two beta sheets(yellow).	+
-		+
-	Observing the <scene name='Sandbox_44/Primary_sequence/1'>Rainbow Coloration</scene> of trypsin one can easily follow the primary sequence of the amino acids as it begins at the amide or N-terminal end(dark blue), and progresses to the carboxyl or C-terminal end with the final 58th amino acid reside (red).	+
-		+
-	Trypsin is also held together by three <scene name='Sandbox_44/Disulfide_bonds/2'>Disulphide Bonds</scene> located between the 5 and 55, 14 and 38, and 30 and 51 Cystine residues(yellow).	+
-		+
-	To determine the polar and non-polar sections of an enzyme, the various R groups coming of of the <scene name='Sandbox_44/Backbone_and_r_groups/2'>protein's backbone</scene> are analyzed. Looking at the <scene name='Sandbox_44/Backbone_and_r_groups/1'>R groups</scene>, the side chains can be classified as either non-polar otherwise known as hydrophobic (literally meaning water fearing) or polar otherwise known as hydrophilic (water loving). Looking first at the	+
-	<scene name='Sandbox_44/Polar_and_nonpolar/1'>ball and stick model</scene> you can easily see the classifications of the nonpolar(pink) and polar(yellow) side chains. Looking at this molecule you can see the majority of the yellow strands are found near the exterior of the enzyme where they would act with the polar enviroment, while many of the nonpolar residues are hidden inside. Looking at the	+
-	<scene name='Sandbox_44/Polar_and_nonpolar_space_fill/1'>space filling</scene> model you can achieve a better grasp on the organization of these nonpolar and polar sections of the enzyme. Polar regions again appear in yellow, nonpolar pink, and some of the waters that would interact with the enzyme appear gray in the diagram.	+
-		+
-	==Function==	+

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Current revision

Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013.

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:

spinqualitylabelsall models Adenylate Kinase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

The of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. The 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 (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 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 (orange) in the center of the protein has (yellow) that allow binding to occur. The (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

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