Sandbox Reserved 1846: Difference between revisions

@@ Line 53: / Line 53: @@
 <scene name='10/1075247/G127/1'>Y127G</scene>
-The original side chain is tyrosine, and is has a mutation to glycine. Like the T96M mutation, it also increases thermostability of the protein, with this mutation Y127G having a melting point of 87.0 degree Celsius. The mutation replaces tyrosine, a bulky, rigid aromatic side chain to glycine, which is the smallest amino acid. This mutation leads to allowing greater flexibility for the protein. By reducing steric hindrance and releasing some strain in the protein structure, allowing for it to be more flexible and more stable at higher temperatures.
+The mutation of tyrosine to glycine at position 127 (Y127G) also increases the protein's thermostability. The mutant melting point is increased to 87.0°C. Tyrosine has a bulky, rigid aromatic side chain that can cause structural strain. Glycine is the smallest amino acid and lacks a side chain, so it provides greater flexibility to the protein. This mutation reduces steric hindrance and relieves strain in the protein structure, therefore allowing it to be more adaptable and stable at higher temperatures. By increasing flexibility, the Y127G mutation helps the protein maintain its folded structure under heat stress.
 === N246 ===

Navigation menu