Sandbox 32
From Proteopedia
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The <scene name='Sandbox_32/Hydrophilic/1'>hydrophilic residues</scene>, highlighted here in blue along with the transparent pink hydrophobic residues, are more towards the outside [is this actually true?] | The <scene name='Sandbox_32/Hydrophilic/1'>hydrophilic residues</scene>, highlighted here in blue along with the transparent pink hydrophobic residues, are more towards the outside [is this actually true?] | ||
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| + | <scene name='Sandbox_32/Water_ligand/1'>Water</scene> also plays a big part in... | ||
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| + | Sidechain and ligand <scene name='Sandbox_32/Sidechain_ligand_interaction/1'>interactions</scene>... | ||
Revision as of 12:50, 17 October 2012
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| 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 (PDB ID #: 1ake)
The by itself may be in a slightly different conformation than when it is attached to the B chain.
Adenylate Kinase contains both types of secondary structure, . In this scene, alpha helices are in light blue and beta sheets are in yellow (the red and blue molecules in the middle are the ligand).
The highlighted in this scene shows us that... something something something. The beta sheets appear to be parallel, as the H-bonds are not all aligned in one direction.
, highlighted here in pink, tend to be towards the inside of the molecule.
The , highlighted here in blue along with the transparent pink hydrophobic residues, are more towards the outside [is this actually true?]
also plays a big part in...
Sidechain and ligand ...
