Sandbox Reserved 1852: Difference between revisions
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===DA_20_10=== | ===DA_20_10=== | ||
====Q162R==== | ====Q162R==== | ||
Residue 162 resides near the top of the binding entrance to the enzyme, and is within 3A in most models on the enzyme. It can act as a hydrogen bond donor to the terminal phosphate on the ligand when in proximity. To increase this interaction, the group chose a Q to <scene name='10/1075254/ | Residue 162 resides near the top of the binding entrance to the enzyme, and is within 3A in most models on the enzyme. It can act as a hydrogen bond donor to the terminal phosphate on the ligand when in proximity. To increase this interaction, the group chose a Q to <scene name='10/1075254/Q_to_r/1'>R mutation</scene>, which decreased the length of the potential hydrogen bond to within 2.5A, increasing the strength of the interaction. | ||
===CE20=== | ===CE20=== | ||
In this generation, it was found that the most catalytically efficient models had mutated T34, P48, and R56 to <scene name='10/1075254/Ce_20_mutations/4'>I43,L48, and S56</scene>. These mutations further tightened the binding pocket and create a more hydrophobic environment. | In this generation, it was found that the most catalytically efficient models had mutated T34, P48, and R56 to <scene name='10/1075254/Ce_20_mutations/4'>I43,L48, and S56</scene>. These mutations further tightened the binding pocket and create a more hydrophobic environment. | ||
