Sandbox 32: Difference between revisions
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The <scene name='Sandbox_32/H_bonds_2/1'>hydrogen bonding</scene> 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. | The <scene name='Sandbox_32/H_bonds_2/1'>hydrogen bonding</scene> 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. | ||
<scene name='Sandbox_32/Hydrophobic_stickandwireframe/1'>Hydrophobic residues</scene>, highlighted here in pink, tend to be towards the inside of the molecule. | |||
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?] | |||
Revision as of 03:48, 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 A Chain 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, alpha helices and beta sheets. 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 hydrogen bonding 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. Hydrophobic residues, highlighted here in pink, tend to be towards the inside of the molecule. The hydrophilic residues, highlighted here in blue along with the transparent pink hydrophobic residues, are more towards the outside [is this actually true?] |
