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Sandbox 32
From Proteopedia
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Trypsin is a medium size globular protein that functions as a pancreatic serine protease. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. | Trypsin is a medium size globular protein that functions as a pancreatic serine protease. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. | ||
==Structure== | ==Structure== | ||
| - | The<scene name='Sandbox_32/N-c_rainbow/2'>pathway</scene> of the protein can be followed from N-terminus of the protein (blue) to the C-terminus of the protein (red). | + | The <scene name='Sandbox_32/N-c_rainbow/2'>pathway</scene> of the protein can be followed from N-terminus of the protein (blue) to the C-terminus of the protein (red). |
Trypsin has many important structural aspects. The <applet scene='Sandbox_32/Secondary_structure/1' size='225' frame='true' align='true' align='right' caption='Trypsin protein with structural aspects shown.'/>secondary structures are shown this figure <scene name='Sandbox_32/Secondary_structure/1'>(Secondary Structure)</scene>. The main backbone of the trypsin protein is shown in yellow <scene name='Sandbox_32/Secondary_structure_main_chain/1'>(main backbone)</scene>. Trypsin has two alpha helices shown in blue <scene name='Sandbox_32/Secondary_structure_alpha/1'>(alpha helices)</scene> and two beta sheets shown in green <scene name='Sandbox_32/Secondary_structure_beta/1'>(beta Sheets)</scene>. The beta sheets in the Trypsin protein are antiparallel to each other and connected by a Beta-hairpin turn. | Trypsin has many important structural aspects. The <applet scene='Sandbox_32/Secondary_structure/1' size='225' frame='true' align='true' align='right' caption='Trypsin protein with structural aspects shown.'/>secondary structures are shown this figure <scene name='Sandbox_32/Secondary_structure/1'>(Secondary Structure)</scene>. The main backbone of the trypsin protein is shown in yellow <scene name='Sandbox_32/Secondary_structure_main_chain/1'>(main backbone)</scene>. Trypsin has two alpha helices shown in blue <scene name='Sandbox_32/Secondary_structure_alpha/1'>(alpha helices)</scene> and two beta sheets shown in green <scene name='Sandbox_32/Secondary_structure_beta/1'>(beta Sheets)</scene>. The beta sheets in the Trypsin protein are antiparallel to each other and connected by a Beta-hairpin turn. | ||
==Polar vs. Nonpolar Residues== | ==Polar vs. Nonpolar Residues== | ||
This image shows the <scene name='Sandbox_32/Polar_versus_nonpolar/2'>polarity</scene> of the residues in the protein. The polar areas of the protein are shown in pink, while the non-polar areas of the molecule are shown in light blue. The polarity of the individual amino acid residues can be seen better in the <scene name='Sandbox_32/Polar_vs_non_stick/1'>stick model</scene>. The polar amino acid residues are again shown in pink, while the non-polar amino acid residues are shown in blue. By rotating the two representations of the polar versus non-polar areas of the protein to an aerial view, it can be seen that the polar (hydrophilic) areas are located toward the outside of the protein, while the non-polar (hydrophobic) areas are located toward the inside of the protein. | This image shows the <scene name='Sandbox_32/Polar_versus_nonpolar/2'>polarity</scene> of the residues in the protein. The polar areas of the protein are shown in pink, while the non-polar areas of the molecule are shown in light blue. The polarity of the individual amino acid residues can be seen better in the <scene name='Sandbox_32/Polar_vs_non_stick/1'>stick model</scene>. The polar amino acid residues are again shown in pink, while the non-polar amino acid residues are shown in blue. By rotating the two representations of the polar versus non-polar areas of the protein to an aerial view, it can be seen that the polar (hydrophilic) areas are located toward the outside of the protein, while the non-polar (hydrophobic) areas are located toward the inside of the protein. | ||
Revision as of 00:24, 25 October 2010
| 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. |
Trypsin
Trypsin is a medium size globular protein that functions as a pancreatic serine protease. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme.
Structure
The of the protein can be followed from N-terminus of the protein (blue) to the C-terminus of the protein (red).
Trypsin has many important structural aspects. The
|
Polar vs. Nonpolar Residues
This image shows the of the residues in the protein. The polar areas of the protein are shown in pink, while the non-polar areas of the molecule are shown in light blue. The polarity of the individual amino acid residues can be seen better in the . The polar amino acid residues are again shown in pink, while the non-polar amino acid residues are shown in blue. By rotating the two representations of the polar versus non-polar areas of the protein to an aerial view, it can be seen that the polar (hydrophilic) areas are located toward the outside of the protein, while the non-polar (hydrophobic) areas are located toward the inside of the protein.
