Sandbox Reserved 1697: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The protein has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. <ref> PMID 33172890 </ref> | |||
There is no quaternary structures in the protein but several tertiary structures that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the proper shape so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules. | There is no quaternary structures in the protein but several tertiary structures that play an important role in the structure of the protein and therefore its function. There are many covalent bonds due to hydrophobic and nonpolar amino acids that form the structure. The amino acids involved with the <scene name='89/892740/Quat_structure_catalytic_amino/1'>catalytic amino acids are mostly polar</scene>, the magnesium ions assist in pulling the enzyme into shape that allow for it to be in the proper shape so that it can dephosphorylate the inositol When the lithium ions interact with the enzyme a shape change occurs that will not allow for the magnesium ions to attach to the enzyme, and therefore the water molecules. | ||
The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape. | The rest of the enzyme is circled around the substrate which allows for a better ability to bind to the substrate, it is shown here how the <scene name='89/892740/Hydrophobic_effect/1'>hydrophobic effect</scene> how the nonpolar and polar amino acids allow for it to have this shape. | ||
