Sandbox Reserved 1846: Difference between revisions

@@ Line 46: / Line 46: @@
 T96M
-The original side chain is threonine and is mutated with a methionine. This is really a mutation that increases thermostability. The wild-type variant has a melting point of 84.7 degree Celsius. The mutation of methionine, is a larger, more hydrophobic side chain, and would contribute to stabilization of the protein's core by increasing hydrophobic interactions. The stronger internal interactions help the enzyme to maintain its folded structure more efficiently at elevated temperatures. Which is shown by the M96 mutation having a melting point of 87.4 degree Celsius.
+The mutation of threonine to methionine at position 96 (M96) increases the protein's thermostability. Threonine has a small, polar side chain, which makes it hydrophilic and less stable at higher temperatures. Methionine, however, has a larger, nonpolar, and hydrophobic side chain, which strengthens hydrophobic interactions in the protein’s core. These stronger internal interactions help stabilize the protein and help it to maintain its folded structure at higher temperatures. As a result, the melting point increases from 84.7°C for the wild-type protein to 87.4°C for the M96 mutant.
 === Y127 ===

Navigation menu