Sandbox 49: Difference between revisions

Line 6:

==Structure==

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. Notice that each of these domains consist of 2 identical subunits. Lipase has an a chain and a b chain that each respectively contain 1 of the subunits of the C Terminal Domain and 1 of the subunits of the N terminal domains, all 4 parts come together to form the fully functional enzyme.

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.

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. Lipase also has a <scene name='Sandbox_49/Ca_ligands/1'>Ca Ligand</scene> that noncovalently binds to residues: Glu 187, Arg 190, Asp 192, Asp 195. There is one Calcium ion bound per chain in the enzyme.

The <scene name='Sandbox_49/Lipase_active_sites_test/1'>Lipase Active Sites</scene> catalytic groups are protected by a flap that folds over the are when a substrate is bound, aiding in the catalytic function of the enzyme.

Sandbox 49: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 6: / Line 6: @@
 ==Structure==
 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. Notice that each of these domains consist of 2 identical subunits. Lipase has an a chain and a b chain that each respectively contain 1 of the subunits of the C Terminal Domain and 1 of the subunits of the N terminal domains, all 4 parts come together to form the fully functional enzyme.
-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.
+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. Lipase also has a <scene name='Sandbox_49/Ca_ligands/1'>Ca Ligand</scene> that noncovalently binds to residues: Glu 187, Arg 190, Asp 192, Asp 195. There is one Calcium ion bound per chain in the enzyme.
+The <scene name='Sandbox_49/Lipase_active_sites_test/1'>Lipase Active Sites</scene> catalytic groups are protected by a flap that folds over the are when a substrate is bound, aiding in the catalytic function of the enzyme.