Sandbox Reserved 1852: Difference between revisions

Line 35:

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.

====A285N====

Residue 285, as follows, is also buried within the binding pocket. The group introduced this mutation to increase steric hindrance with the catalytic tyrosine, reducing the number of rotamers the residue has to increase the reactivity of the enzyme by lowering the distance between Y134 and the ligand.

<scene name='10/1075254/N285/1'>Residue 285</scene>, as follows, is also buried within the binding pocket. The group introduced this mutation to increase steric hindrance with the catalytic tyrosine, reducing the number of rotamers the residue has to increase the reactivity of the enzyme by lowering the distance between Y134 and the ligand.

===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.

Sandbox Reserved 1852: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 35: / Line 35: @@
 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.
 ====A285N====
-Residue 285, as follows, is also buried within the binding pocket. The group introduced this mutation to increase steric hindrance with the catalytic tyrosine, reducing the number of rotamers the residue has to increase the reactivity of the enzyme by lowering the distance between Y134 and the ligand.
+<scene name='10/1075254/N285/1'>Residue 285</scene>, as follows, is also buried within the binding pocket. The group introduced this mutation to increase steric hindrance with the catalytic tyrosine, reducing the number of rotamers the residue has to increase the reactivity of the enzyme by lowering the distance between Y134 and the ligand.
 ===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.