Sandbox Reserved 192: Difference between revisions
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=='''Further Research'''== | =='''Further Research'''== | ||
''Replacement of Phe46'': 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 x-ray crystallographic structures were determined in an attempt 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. But this has no effect on the substrates ability to bind. The core itself is very limited to adjusting to changes because of its limited mobility from the study di-sulfide bonds | ''Replacement of Phe46'': The phenylalanine-46 (<scene name='Sandbox_Reserved_192/Phe_46b/1'>Phe46</scene>) residue located within the hydrophobic core of RNase A was experimentally replaced with other hydrophobic residues; leucine, valine and alanine. The x-ray crystallographic structures were determined in an attempt 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. But this has no effect on the substrates ability to bind. The core itself is very limited to adjusting to changes because of its limited mobility from the study di-sulfide bonds | ||
=='''Evolutionary Significance'''== | =='''Evolutionary Significance'''== | ||
