Sandbox 49: Difference between revisions

Line 9:

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.

Important for the tertiary structure of the protein, are several different factors that function to hold each of the domains together in the proper orientation, 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.

Sandbox 49: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 9: / Line 9: @@
 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.
+Important for the tertiary structure of the protein, are several different factors that function to hold each of the domains together in the proper orientation, 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.