Sandbox 31: Difference between revisions

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Adenylate kinase is caged with <scene name='Sandbox_31/Ak_waters/1'>water molecules</scene>.  
Adenylate kinase is caged with <scene name='Sandbox_31/Ak_waters/1'>water molecules</scene>.  
==I can add headings==


This is the <scene name='Sandbox_31/Ak_main/1'>AK</scene> scene.
This is the <scene name='Sandbox_31/Ak_main/1'>AK</scene> scene.


==Structure==
==Structure==
The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). Adenylate kinase has a <scene name='Sandbox_31/Ak_hydrophilic/1'>hydrophilic</scene> exterior, and a  <scene name='Sandbox_31/Ak_hydrophobic/1'>hydrophobic</scene> core, with additional  
The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). A network of <scene name='Sandbox_31/Ak_hydrogen_bonds/1'>hydrogen bonds</scene> hold the secondary structural elements together. You can see the regular hydrogen bonding pattern in the alpha helices.
 
Adenylate kinase has a <scene name='Sandbox_31/Ak_hydrophilic/1'>hydrophilic</scene> exterior, and a  <scene name='Sandbox_31/Ak_hydrophobic/1'>hydrophobic</scene> core, with additional  
<scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand.  
<scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand.  
   
   
<scene name='Sandbox_31/Ak_2nd_structure/1'>helix and sheet</scene>
==Active Site and Mechanism==
==Active Site and Mechanism==


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<references/>
<references/>
<scene name='Sandbox_31/Rhodopsin_ball_and_chain/1'>Rhodopsin ball and stick</scene>