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Sandbox 50
From Proteopedia
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==Structure == | ==Structure == | ||
Horse pancreatic lipase contains two identical peptide chains containing 449 amino acid residues. The N to C terminal order is shown <scene name='Sandbox_50/5-3_rainbow/1'>here</scene> where the N terminus is in blue and can be followed to the C terminus in red. Each chain contains | Horse pancreatic lipase contains two identical peptide chains containing 449 amino acid residues. The N to C terminal order is shown <scene name='Sandbox_50/5-3_rainbow/1'>here</scene> where the N terminus is in blue and can be followed to the C terminus in red. Each chain contains | ||
| - | <scene name='Sandbox_50/N_and_c_terminus/1'>two well defined domains</scene>. The N-terminal domain is shown in blue and the C terminal domain is shown in green. The active site of HPL is highlighted in red to show its location in the N terminal domain of the A chain. | + | <scene name='Sandbox_50/N_and_c_terminus/1'>two well defined domains</scene>. The N-terminal domain is shown in blue and the C terminal domain is shown in green. The active site of HPL is highlighted in red to show its location in the N terminal domain of the A chain. Additionally, the <scene name='Sandbox_50/Aa_types/1'>charge distribution</scene> can be seen here where negatively charged amino acid residues are seen in red, and positively charged amino acids are seen in blue. |
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 residues</scene> in pink point congregate more on the exterior and point outwards. | <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/Aa_types/1'>charge and polarity</scene> | ||
Revision as of 00:07, 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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