Sandbox Reserved 1852

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Residue 284 resides deep within the binding pocket of the enzyme. The group chose an <scene name='10/1075253/S284/2'>S</scene> to <scene name='10/1075253/A285_scence/2'>A</scene> mutation to increase the hydrophobicity of the binding pocket and reduce reactivity, without also changing any steric characteristics in the region ''unintentionally'' near the catalytic residues.
Residue 284 resides deep within the binding pocket of the enzyme. The group chose an <scene name='10/1075253/S284/2'>S</scene> to <scene name='10/1075253/A285_scence/2'>A</scene> mutation to increase the hydrophobicity of the binding pocket and reduce reactivity, without also changing any steric characteristics in the region ''unintentionally'' near the catalytic residues.
=====A285N=====
=====A285N=====
-
:<scene name='10/1075254/N285/2'>N285</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.
+
:<scene name='10/1075254/N285/3'>N285</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.
===CE6===
===CE6===
The DA_20_10 model of the Diels Alderase was further enhanced by players of the online game "Foldit." Building on preliminary early data, players were asked to optimize various helical structures that would surround and support the ligand. After over 100,000 designs were tested, the top-scoring CE6 model was finalized, containing as <scene name='10/1075252/Alpha_helix_highlighted/4'>alpha helix cap</scene> that favorably constrains ligand orientation. This "cap" consists of two helices--helix one spans from residues 36-44, and helix two spans from residues 48-56.
The DA_20_10 model of the Diels Alderase was further enhanced by players of the online game "Foldit." Building on preliminary early data, players were asked to optimize various helical structures that would surround and support the ligand. After over 100,000 designs were tested, the top-scoring CE6 model was finalized, containing as <scene name='10/1075252/Alpha_helix_highlighted/4'>alpha helix cap</scene> that favorably constrains ligand orientation. This "cap" consists of two helices--helix one spans from residues 36-44, and helix two spans from residues 48-56.

Revision as of 23:48, 15 April 2025

This Sandbox is Reserved from March 18 through September 1, 2025 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson and Mark Macbeth at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1828 through Sandbox Reserved 1846.
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Diels-Alderase

Diels-Alderase 4o5t

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