CHEM2052 Tutorial: Difference between revisions

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This arrangement of amino acids is also called a '''charge relay system''' <ref>PMID: 7016210</ref>.  
This arrangement of amino acids is also called a '''charge relay system''' <ref>PMID: 7016210</ref>.  


Now compare the active site residues of chymotrypsin to the <scene name='59/596400/Morph/2'>trypsin catalytic triad and the elastase catalytic triad</scene> (trypsin is PDB code [[1aq7]] and elastase is PDB code [[4est]].
Now compare the active site residues of chymotrypsin to the <scene name='59/596400/Morph/3'>trypsin catalytic triad and the elastase catalytic triad</scene> (<span style="color:lightblue;background-color:black;font-weight:bold;">trypsin is in light blue</span>, PDB code [[1aq7]] and <span style="color:pink;background-color:black;font-weight:bold;">elastase is in pink</span>, PDB code [[4est]]). <jmol><jmolButton><script>frame next</script><text>Click this button</text></jmolButton></jmol> to flip between structures.
{{Template:Button Toggle Animation2}}
 
== '''Substrate Binding Pockets''' ==
== '''Substrate Binding Pockets''' ==
The next links examine the binding pockets of each protein. The spacefilled residues have been color coded according to hydrophobicity (residues are indicated as: {{Template:ColorKey_Hydrophobic}} or {{Template:ColorKey_Polar}}, with <font color="FF0000">'''Aspartate'''</font> highlighted further ).
The next links examine the binding pockets of each protein. The spacefilled residues have been color coded according to hydrophobicity (residues are indicated as: {{Template:ColorKey_Hydrophobic}} or {{Template:ColorKey_Polar}}, with <font color="FF0000">'''Aspartate'''</font> highlighted further ).
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== '''Understanding the Mechanism''' ==
== '''Understanding the Mechanism''' ==
==== '''Catalytic Mechanism''' ====
==== '''Catalytic Mechanism''' ====
Lehninger's Principles of Biochemistry (5th edition)describes the catalytic mechanism of chymotrypsin on pages 208-209. An [http://bcs.whfreeman.com/lehninger5e/pages/bcs-main.asp?v=&s=06000&n=00010&i=06010.01&o=|00610|00580|00590|00510|00540|00600|00550|00570|00630|00010|00020|00030|00040|00070|00080|00090|00100|01000|02000|03000|04000|05000|06000|07000|08000|09000|10000|11000|12000|13000|14000|15000|16000|17000|18000|19000|20000|21000|22000|23000|24000|25000|26000|27000|28000|99000| animated version] of the enzyme-catalyzed hydrolysis reaction is also available on the textbook's website. <scene name='User:Amy_Kerzmann/Sandbox_5/New_chymotrypsin-triad/10'>
The following animation describes the catalytic mechanism of chymotrypsin [http://www.sumanasinc.com/webcontent/animations/content/chymotrypsin.html]. <scene name='User:Amy_Kerzmann/Sandbox_5/New_chymotrypsin-triad/10'>


This representation</scene> was designed to match the perspective given by those resources. To provide better orientation after this rotation, here are the <scene name='User:Amy_Kerzmann/Sandbox_5/New_chymotrypsin-triad/11'>binding pocket residues</scene> that were highlighted above. (Or you can <scene name='User:Amy_Kerzmann/Sandbox_5/New_chymotrypsin-triad/16'>label the catalytic triad and Gly193</scene>.)
This representation</scene> was designed to match the perspective given by those resources. To provide better orientation after this rotation, here are the <scene name='User:Amy_Kerzmann/Sandbox_5/New_chymotrypsin-triad/11'>binding pocket residues</scene> that were highlighted above. (Or you can <scene name='User:Amy_Kerzmann/Sandbox_5/New_chymotrypsin-triad/16'>label the catalytic triad and Gly193</scene>.)

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Avril Robertson, Alexander Berchansky, Jaime Prilusky