Sandbox Reserved 1846: Difference between revisions

The mutation of Tyr to Gly at <scene name='10/1075247/Y127/4'>Tyr127</scene> also increases the thermostability, <scene name='10/1075247/Original_15_mutation_structure/6'>Reference Tyr127</scene>. The melting point of Y127G is increased to 87.0°C from the WT melting point of 84.7°C. Tyr has a bulky, rigid aromatic side chain that can cause structural strain, shown in <scene name='10/1075247/Y127_spacefill/1'>Y127 representation</scene>. Gly is the smallest amino acid and lacks a side chain, providing greater flexibility. The mutation <scene name='10/1075247/Y127g/2'>Y127G</scene> melting point is increased to 87.0°C. The mutation reduces [https://en.wikipedia.org/wiki/Steric_effects#:~:text=Steric%20hindrance%20is%20the%20slowing,as%20slowing%20unwanted%20side%2Dreactions. steric hindrance] and relieves strain in the protein structure, demonstrated in <scene name='10/1075247/Y127g_space_fill/1'>Y127G representation</scene>. By increasing flexibility, the Y127G mutation helps the protein maintain its folded structure under heat stress.<ref name="Tournier"/>