Sandbox 50: Difference between revisions

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The <scene name='Sandbox_50/Ak_secondary_structure/1'>secondary_structure</scene> of the protein contains 12 alpha helices (yellow) and 7 beta sheets (green). This secondary structure is held together by <scene name='Sandbox_50/Ak_hydrogen_bonds/1'>hydrogen_bonds</scene>, which are anti-parallel between the beta sheets.

==~~Residues~~==

==Hydrophobic and Hydrophilic Residue Composition==

The <scene name='Sandbox_50/Ak_hydrophobic_residues/1'>hydrophobic_residues</scene> of ADK, seen in gray, is buried in the interior of the protein. While the <scene name='Sandbox_50/~~Ak_hydrophilic_residues1~~/1'>hydrophilic_residues</scene>, all the charged and polar side chains (purple), are on the surface of the protein and exposed. The location of the residues depend on the solvent and the environment that the protein is found in. All the hydrophobic residues aggregate together, and bury themselves in the interior of the protein to minimize their contact with their environment. The hydrophilic residues, on the other hand, is exposed on the surface because the enzyme is in an hydrophilic environment. Although, most of the hydrophilic residues would be exposed, it is possible for some of the to be buried in the interior, but they would interact with each other be stabilized there. There are also hydrophilic residues in the active site of the enzyme, where the ligand binds, to help it enter so that the reaction can take place.

The <scene name='Sandbox_50/Ak_hydrophobic_residues/1'>hydrophobic_residues</scene> of ADK, seen in gray, is buried in the interior of the protein. While the <scene name='Sandbox_50/Ak_hydrophiblic_residues2/1'>hydrophilic_residues</scene>, all the charged and polar side chains (purple), are on the surface of the protein and exposed. The location of the residues depend on the solvent and the environment that the protein is found in. All the hydrophobic residues aggregate together, and bury themselves in the interior of the protein to minimize their contact with their environment. The hydrophilic residues, on the other hand, is exposed on the surface because the enzyme is in an hydrophilic environment. Although, most of the hydrophilic residues would be exposed, it is possible for some of the to be buried in the interior, but they would interact with each other be stabilized there. There are also hydrophilic residues in the active site of the enzyme, where the ligand binds, to help it enter so that the reaction can take place.

==Active Site==

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<scene name='Sandbox_50/Ak_hydrophilic_residues/1'>hydrophilic_residues</scene>

<scene name='Sandbox_50/Ak_hydrophobic1/1'>TextToBeDisplayed</scene>

<scene name='Sandbox_50/Ak_alpha_helices/1'>alpha_helices</scene>

<scene name='Sandbox_50/Ak_beta_sheets/1'>beta_sheets</scene>

Sandbox 50: Difference between revisions

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@@ Line 13: / Line 13: @@
 The <scene name='Sandbox_50/Ak_secondary_structure/1'>secondary_structure</scene> of the protein contains 12 alpha helices (yellow) and 7 beta sheets (green). This secondary structure is held together by <scene name='Sandbox_50/Ak_hydrogen_bonds/1'>hydrogen_bonds</scene>, which are anti-parallel between the beta sheets.
-==Residues==
+==Hydrophobic and Hydrophilic Residue Composition==
-The <scene name='Sandbox_50/Ak_hydrophobic_residues/1'>hydrophobic_residues</scene> of ADK, seen in gray, is buried in the interior of the protein. While the <scene name='Sandbox_50/Ak_hydrophilic_residues1/1'>hydrophilic_residues</scene>, all the charged and polar side chains (purple), are on the surface of the protein and exposed. The location of the residues depend on the solvent and the environment that the protein is found in. All the hydrophobic residues aggregate together, and bury themselves in the interior of the protein to minimize their contact with their environment. The hydrophilic residues, on the other hand, is exposed on the surface because the enzyme is in an hydrophilic environment. Although, most of the hydrophilic residues would be exposed, it is possible for some of the to be buried in the interior, but they would interact with each other be stabilized there. There are also hydrophilic  residues in the active site of the enzyme, where the ligand binds, to help it enter so that the reaction can take place.
+The <scene name='Sandbox_50/Ak_hydrophobic_residues/1'>hydrophobic_residues</scene> of ADK, seen in gray, is buried in the interior of the protein. While the <scene name='Sandbox_50/Ak_hydrophiblic_residues2/1'>hydrophilic_residues</scene>, all the charged and polar side chains (purple), are on the surface of the protein and exposed. The location of the residues depend on the solvent and the environment that the protein is found in. All the hydrophobic residues aggregate together, and bury themselves in the interior of the protein to minimize their contact with their environment. The hydrophilic residues, on the other hand, is exposed on the surface because the enzyme is in an hydrophilic environment. Although, most of the hydrophilic residues would be exposed, it is possible for some of the to be buried in the interior, but they would interact with each other be stabilized there. There are also hydrophilic  residues in the active site of the enzyme, where the ligand binds, to help it enter so that the reaction can take place.
 ==Active Site==
@@ Line 27: / Line 27: @@
 <scene name='Sandbox_50/Ak_hydrophilic_residues/1'>hydrophilic_residues</scene>
+<scene name='Sandbox_50/Ak_hydrophobic1/1'>TextToBeDisplayed</scene>
 <scene name='Sandbox_50/Ak_alpha_helices/1'>alpha_helices</scene>
 <scene name='Sandbox_50/Ak_beta_sheets/1'>beta_sheets</scene>