Sandbox 49: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 2: | Line 2: | ||
=Introduction= | =Introduction= | ||
Lipase is an enzyme that functions to convert triacylglycerols to 2-monoacylglycerols, it catalyzes the reaction to break down lipids into its subunits. Lipase has 449 amino acid resiudes, and 2 domains, the <scene name='Sandbox_49/C_terminal_domains/1'>C Terminal Domains</scene> is smaller with 112 residues, and the <scene name='Sandbox_49/N_terminal_domain_1/1'>N Terminal Domain</scene> consists of 337 residues. The secondary structural elements of Lipase, including the name='Sandbox_49/Beta_sheets_test_1/1'>Beta Sheets</scene> that make up 30 percent of the amino acid chain, and involving 139 residues as well as the <scene name='Sandbox_49/Alpha_helices_1/1'>Alpha Helices</scene> that make up 22 percent and 102 residues characterize the structure of the protein. | Lipase is an enzyme that functions to convert triacylglycerols to 2-monoacylglycerols, it catalyzes the reaction to break down lipids into its subunits. Lipase has 449 amino acid resiudes, and 2 domains, the <scene name='Sandbox_49/C_terminal_domains/1'>C Terminal Domains</scene> is smaller with 112 residues, and the <scene name='Sandbox_49/N_terminal_domain_1/1'>N Terminal Domain</scene> consists of 337 residues. The secondary structural elements of Lipase, including the <scene name='Sandbox_49/Beta_sheets_test_1/1'>Beta Sheets</scene> that make up 30 percent of the amino acid chain, and involving 139 residues as well as the <scene name='Sandbox_49/Alpha_helices_1/1'>Alpha Helices</scene> that make up 22 percent and 102 residues characterize the structure of the protein. | ||