Sandbox 31: Difference between revisions

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{{Template:Oberholser_Sandbox_Reservation}}
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== '''Adenylate Kinase'''  (PDB ID #: 1ake)==
<Structure load='1ake' size='500' frame='true' align='right' caption='adenylate kinase bound to non-hydrolyzable substrate analogue' scene='Insert optional scene name here' />


== '''Adenylate Kinase'''  (PDB ID #: 1ake)==
<Structure load='Insert PDB code or filename here' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_31/Primary_scene/2' />


==Introduction==
==Introduction==
   
   
<scene name='Sandbox_31/Adenylate_kinase/1'>Adenylate Kinase</scene>
<scene name='Sandbox_31/Adenylate_kinase/2'>Adenylate Kinase</scene>
is a good little protein.  
is a good little protein.  


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==Physical Properties==
==Physical Properties==


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.


==Structure==
==Structure==
the <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha helicies (cyan) and beta sheets (green) surrounding the non-hydrolyzable substrate analogue (orange).  
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_2nd_structure/1'>helix and sheet</scene>
==Active Site and Mechanism==
==Active Site and Mechanism==


residues within <scene name='Sandbox_31/Ak_ligand_binding/3'>3 angstroms</scene> of the ligand are involved in binding the ligand or stabilizing the active site.


adenylate kinase's <scene name='Sandbox_31/Ak_active_site/1'>active site</scene> is highlighted in dark blue.


together you can see that the <scene name='Sandbox_31/Ak_ligand_binding_and_active_s/1'>active site</scene> is only a fraction of the molecules involved in binding the ligand.


<Structure load='3be4' size='500' frame='true' align='right' caption='Cryptosporidium parvum' scene='adenylate kinase' />


 
Comparing the E.coli structure to <scene name='Sandbox_31/Ak_cryptosporidium_parvum/1'>Cryptosporidium parvum</scene>
==References==
==References==


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