Sandbox Reserved 192: Difference between revisions
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=='''Further Research with the Hydrophobic Core'''== | =='''Further Research with the Hydrophobic Core'''== | ||
The phenylalanine-46 (Phe46) residue located within the hydrophobic core of RNase A was experimentally replaced with other hydrophobic residues; leucine, valine and alanine. The goal was to conclude how the change would affect the conformational stability. It was concluded that the replacement of Phe46, which is key to the formation of the hydrophobic core, causes the destabilization of the RNase A by preventing the core from being tightly packed. The amino acids that are hyhdrophobic are; valine, isoleucine, leucine, methionine, phenylalanine, tryptophan and cysteine. The protein folds with its hydrophobic amino acids facing inward and its hydrophilic amino acids facing outward to reduce the amount of water that interacts with the least number of hydrophobic residues (Kadonosono). | The phenylalanine-46 (Phe46) residue located within the <scene name='Sandbox_Reserved_192/Hydrophobic_core/1'>hydrophobic core</scene> of RNase A was experimentally replaced with other hydrophobic residues; leucine, valine and alanine. The goal was to conclude how the change would affect the conformational stability. It was concluded that the replacement of Phe46, which is key to the formation of the hydrophobic core, causes the destabilization of the RNase A by preventing the core from being tightly packed. The amino acids that are hyhdrophobic are; valine, isoleucine, leucine, methionine, phenylalanine, tryptophan and cysteine. The protein folds with its hydrophobic amino acids facing inward and its hydrophilic amino acids facing outward to reduce the amount of water that interacts with the least number of hydrophobic residues (Kadonosono). | ||
=='''Evolutionary Significance'''== | =='''Evolutionary Significance'''== | ||