Sandbox Reserved 1845: Difference between revisions
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<scene name='10/1075247/Y127/4'>Y127</scene> | <scene name='10/1075247/Y127/4'>Y127</scene> | ||
<scene name='10/1075247/Y127g/ | <scene name='10/1075247/Y127g/2'>Y127G</scene> | ||
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. | 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. | ||
