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Sandbox 50
From Proteopedia
(Difference between revisions)
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The <scene name='Sandbox_50/Helix/2'>secondary structure</scene> of HPL contains 13 alpha helices and 28 strands of beta sheets, representing 22% and 30%, respectively, of the protein's residues. Hydrophic collapse contributes to much of the secondary and tertiary structures, as the | The <scene name='Sandbox_50/Helix/2'>secondary structure</scene> of HPL contains 13 alpha helices and 28 strands of beta sheets, representing 22% and 30%, respectively, of the protein's residues. Hydrophic collapse contributes to much of the secondary and tertiary structures, as the | ||
| - | <scene name='Sandbox_50/Hphobic_residues/2'>hydrophobic residues</scene> shown in grey are mostly facing towards the interior of the protein. Conversely, the <scene name='Sandbox_50/Polar_residues/2'>polar | + | <scene name='Sandbox_50/Hphobic_residues/2'>hydrophobic residues</scene> shown in grey are mostly facing towards the interior of the protein. Conversely, the <scene name='Sandbox_50/Polar_residues/2'>polar residues</scene> in pink point congregate more on the exterior and point outwards. |
=== test === | === test === | ||
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| - | <scene name='Sandbox_50/Hphobic_residues/2'>h phobic facing in in gray</scene> | ||
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| - | <scene name='Sandbox_50/Polar_residues/2'>pink polar residue out</scene> | ||
Revision as of 00:01, 14 November 2011
| 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. |
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