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User:Amy Kerzmann/Sandbox 5
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| - | <table width=' | + | <table width='900' align='center' cellpadding='2'><td rowspan='2'> </td><td bgcolor='#eeeeee'> |
| - | <center>'''Chymotrypsin''', resolution 2.00 Å (<scene name='User:Amy_Kerzmann/Sandbox_5/ | + | <center>'''Chymotrypsin''', resolution 2.00 Å (<scene name='User:Amy_Kerzmann/Sandbox_5/New_chymotrypsin-triad/2'>initial scene</scene>). </center><applet load='2cha' size='300' frame='true' align='left' scene='User:Amy_Kerzmann/Sandbox_5/New_chymotrypsin-triad/2' /></td><td bgcolor='#eeeeee'> |
<center>'''Trypsin''', resolution 1.34 Å (<scene name='User:Amy_Kerzmann/Sandbox_5/New_trypsin-wt-triad/4'>initial scene</scene>).</center><applet load='1aq7' size='300' frame='true' align='center' scene='User:Amy_Kerzmann/Sandbox_5/New_trypsin-wt-triad/4'/></td><td bgcolor='#eeeeee'> | <center>'''Trypsin''', resolution 1.34 Å (<scene name='User:Amy_Kerzmann/Sandbox_5/New_trypsin-wt-triad/4'>initial scene</scene>).</center><applet load='1aq7' size='300' frame='true' align='center' scene='User:Amy_Kerzmann/Sandbox_5/New_trypsin-wt-triad/4'/></td><td bgcolor='#eeeeee'> | ||
<center>'''Elastase''', resolution 1.78 Å (<scene name='User:Amy_Kerzmann/Sandbox_5/New_elastase-triad/3'>initial scene</scene>).</center><applet load='4est' size='300' frame='true' align='right' scene='User:Amy_Kerzmann/Sandbox_5/New_elastase-triad/3'/></td><td bgcolor='#eeeeee'></td></table> | <center>'''Elastase''', resolution 1.78 Å (<scene name='User:Amy_Kerzmann/Sandbox_5/New_elastase-triad/3'>initial scene</scene>).</center><applet load='4est' size='300' frame='true' align='right' scene='User:Amy_Kerzmann/Sandbox_5/New_elastase-triad/3'/></td><td bgcolor='#eeeeee'></td></table> | ||
| - | Serine proteases perform their catalytic roles using three key residues: Ser, His, Asp. Because the proteases utilize these three residues for function, they are referred to as the '''catalytic triad'''. Highlight the <scene name='User:Amy_Kerzmann/Sandbox_5/ | + | Serine proteases perform their catalytic roles using three key residues: Ser, His, Asp. Because the proteases utilize these three residues for function, they are referred to as the '''catalytic triad'''. Highlight the <scene name='User:Amy_Kerzmann/Sandbox_5/New_chymotrypsin-triad/1' target='0'>chymotrypsin catalytic triad</scene>. Mouse over the structure to determine the residue numbers for Ser, Asp and His. |
Revision as of 10:08, 10 February 2010
Serine Proteases
The most famous members of the serine protease family are trypsin, chymotrypsin and elastase. These digestive enzymes are also useful tools in biochemistry and molecular biology to ascertain protein sequences.
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Serine proteases perform their catalytic roles using three key residues: Ser, His, Asp. Because the proteases utilize these three residues for function, they are referred to as the catalytic triad. Highlight the . Mouse over the structure to determine the residue numbers for Ser, Asp and His.
Now compare chymotrypsin to . The .
The contains Asp189 to select for positively charged sidechains.
The contains Gly190, Val216 and Thr226.
By highlighting the solvent-accessible surfaces of and , one can better understand why trypsin has specificity for large, charged sidechains whereas elastase targets smaller residues.
