Sandbox 39: Difference between revisions
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== Primary, Secondary, and Tertiary Structure == | == Primary, Secondary, and Tertiary Structure == | ||
Papain is composed of 212 amino acid residues that make up its primary structure. | Papain is composed of 212 amino acid residues that make up its primary structure. | ||
Papain's primary structure causes it to fold into different motifs that make up its secondary structure. These motifs include <scene name='Sandbox_39/Alpha_helices/2'>alpha helices</scene>, shown in green, and <scene name='Sandbox_39/Beta_pleated_sheets/2'>beta pleated sheets</scene>, shown in orange. As shown to the left, papain has 7 alpha helices and 8 beta pleated sheets. All other motifs are nonrandom, structural units, mostly simply turns. | Papain's primary structure causes it to fold into different motifs that make up its secondary structure. These motifs include <scene name='Sandbox_39/Alpha_helices/2'>alpha helices</scene>, shown in green, and <scene name='Sandbox_39/Beta_pleated_sheets/2'>beta pleated sheets</scene>, shown in orange. As shown to the left, papain has 7 alpha helices and 8 beta pleated sheets. All other motifs are nonrandom, structural units, mostly simply turns. | ||
Papain's seconary structures then fold even further to for its three-dimensional structure, which consists of two distinct structural domains with a cleft between them. This cleft contains the catalytic diad discussed above. This tertiary structure is pictured to the right. | Papain's seconary structures then fold even further to for its three-dimensional structure, which consists of two distinct structural domains with a cleft between them. This cleft contains the catalytic diad discussed above. This tertiary structure is pictured to the right. | ||
[[Image:9pap moreau 1.jpeg|right]] | [[Image:9pap moreau 1.jpeg|right]] | ||
<ref>Image from: | <ref>Image from: | ||
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3. Hans-Hartwig Otto, and Tanja Schirmeister (1997) Cysteine Proteases and Their Inhibitors. Chemical Reviews. No. 97, 133-171. | 3. Hans-Hartwig Otto, and Tanja Schirmeister (1997) Cysteine Proteases and Their Inhibitors. Chemical Reviews. No. 97, 133-171. | ||
4 | 4. Image from: http://linus.chem.ku.edu/hewlett/Chem188/Enzyme/enzyme_background.htm | ||
5. Image from: http://www.rcsb.org/pdb/explore/jmol.do?structureId=9PAP&bionumber=1 | |||
6. Image from: http://www.rcsb.org/pdb/explore/explore.do?structureId=1POP | |||
