Sandbox 49

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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. The protein is held together by a combination of several factors, the <scene name='Sandbox_49/Lipase_hydrohpobic_residues/1'>hydrophobic residues</scene> certainly make a difference as one might expect, since all proteins generally fold to shield these from interaction with water, the cysteine residues that Lipase has also play a major role since they form <scene name='Sandbox_49/Disulfide_bonds/1'>Disulfide Bonds</scene>, Lipase has 12 disulfide bonds in all.

 

 

 

 

<scene name='Sandbox_49/Lipase_hydrohpobic_residues/1'>hydrophobic residues</scene>

 

<scene name='Sandbox_49/Lipase_active_sites_test/1'>Lipase Active Sites</scene>

 

<scene name='Sandbox_49/Alpha_helices_1/1'>Alpha Helices</scene>

 

<scene name='Sandbox_49/Beta_sheets_test_1/1'>Beta Sheets</scene>

 

<scene name='Sandbox_49/Turns_1/1'>Turns</scene>

 

 

 

 

 

<scene name='Sandbox_49/Disulfide_bonds/1'>Disulfide Bonds</scene>