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Sandbox 45

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<applet load='3LJJ' size='300' frame='true' align='right' caption='Bovine Trypsin' />
 
= Structure of Trypsin =
= Structure of Trypsin =
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<scene name='Sandbox_45/Helixhold_vanderwaals/1'>van der Waals forces</scene>
<scene name='Sandbox_45/Helixhold_vanderwaals/1'>van der Waals forces</scene>
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<applet load='3LJJ' size='300' frame='true' align='right' caption='Bovine Trypsin' />
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<scene name='Sandbox_45/Bt-phillic/1'>hydrophilic residues</scene>
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<scene name='Sandbox_45/Bt-phillic/3'>hydrophobic residues</scene>
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<scene name='Sandbox_45/Bt-phillic_waters/2'>water interaction</scene>
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<scene name='Sandbox_45/Bt-phillic_waters/3'>transparent</scene>
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== Ligand Binding and Catalysis ==
<scene name='Sandbox_45/Btligand/1'>ligands</scene>
<scene name='Sandbox_45/Btligand/1'>ligands</scene>
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[[Image:Ligandinteractionstrypsin.gif|thumb|center|upright=2.0]]
[[Image:Ligandinteractionstrypsin.gif|thumb|center|upright=2.0]]
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<scene name='Sandbox_45/Catalytic_triad/1'>catalytic triad</scene>
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<scene name='Sandbox_45/Bt-phillic/1'>hydrophilic residues</scene>
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<scene name='Sandbox_45/Bt-phillic/3'>hydrophobic residues</scene>
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<scene name='Sandbox_45/Bt-phillic_waters/2'>water interaction</scene>
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<scene name='Sandbox_45/Bt-phillic_waters/3'>transparent</scene>
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Revision as of 01:21, 29 October 2010

Contents

Structure of Trypsin



Primary

Bovine trypsin contains 223 amino acid residues of varied interactive tendencies and chemical characteristics, each of which contribute to the protein's structure and catalytic function.

Secondary

The spacial arrangement of hydrophobic and hydrophilic residues


sig of disulfides in overall structure, helix to beta sheet,

Bovine Trypsin

Drag the structure with the mouse to rotate

Ligand Binding and Catalysis

key amino acids

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