Sandbox 34: Difference between revisions
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<Structure load='1ake' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Awesomeness' /> | <Structure load='1ake' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Awesomeness' /> | ||
<scene name='Sandbox_34/Adenylate_kinase/1'>Adenylate Kinase</scene> is a very important protein in many biological processes, especially monitoring metabolism. | <scene name='Sandbox_34/Adenylate_kinase/1'>Adenylate Kinase</scene> is a very important protein in many biological processes, especially monitoring metabolism. | ||
Adenylate Kinase is made up of <scene name='Sandbox_34/Adenylate_kinase_colors/1'>9 beta sheets (light blue) and 9 alpha helices (dark blue).</scene> These are very important for the conformation and function of the enzyme. The sheets are parallel in the protein which puts extra strain on the <scene name='Sandbox_34/Adenylate_kinase_hbonds_yell/1'>hydrogen bonds (yellow)</scene> within the protein. These bonds are also very important in that they help to hold the helices and sheets together. These hydrogen bonds are formed from interactions among the proteins many hydrogen containing residues. Without them the protein would unravel and denature. | Adenylate Kinase is made up of <scene name='Sandbox_34/Adenylate_kinase_colors/1'>9 beta sheets (light blue) and 9 alpha helices (dark blue).</scene> These are very important for the conformation and function of the enzyme. The beta sheets are parallel in the protein which puts extra strain on the <scene name='Sandbox_34/Adenylate_kinase_hbonds_yell/1'>hydrogen bonds (yellow)</scene> within the protein. That is why there appear to be angled in stead of straight (which is found in anti-parallel beta sheets). These bonds are also very important in that they help to hold the helices and sheets together. These hydrogen bonds are formed from interactions among the proteins many hydrogen containing residues. Without them the protein would unravel and denature. | ||
The <scene name='Sandbox_34/Adenylate_kinasehydrophobic_go/3'>hydrophobic interactions (deep pink)</scene> also play a huge role in holding this protein together. These interactions are formed by the hydrophobic or non-polar residues of the proteins. | The <scene name='Sandbox_34/Adenylate_kinasehydrophobic_go/3'>hydrophobic interactions (deep pink)</scene> also play a huge role in holding this protein together. These interactions are formed by the hydrophobic or non-polar residues of the proteins. | ||
However, the hydrophobic interactions are not the only thing holding it together or helping to keep its conformation. There are also many <scene name='Sandbox_34/Adenylate_kinase_andpolarside/1'>polar and charged side groups (green)</scene> that help maintain the hydrophobic interactions and help stabilize the protein by interacting with one another. The interaction between the polar groups and the hydrophobic groups can be seen by the pink transparent hydrophobic groups and the green polar groups. | However, the hydrophobic interactions are not the only thing holding it together or helping to keep its conformation. There are also many <scene name='Sandbox_34/Adenylate_kinase_andpolarside/1'>polar and charged side groups (green)</scene> that help maintain the hydrophobic interactions and help stabilize the protein by interacting with one another. The interaction between the polar groups and the hydrophobic groups can be seen by the pink transparent hydrophobic groups and the green polar groups. | ||