Sandbox Reserved 807
From Proteopedia
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<scene name='56/563219/Hydrophobic_residues/1'>Hydrophobic Residues</scene> are shown in gray. These residues prefer little to no contact with water, and so typically hide in the interior of the protein | <scene name='56/563219/Hydrophobic_residues/1'>Hydrophobic Residues</scene> are shown in gray. These residues prefer little to no contact with water, and so typically hide in the interior of the protein | ||
| - | <scene name='56/563219/Hydrophilic_residues/1'> | + | <scene name='56/563219/Hydrophilic_residues/1'>Hydrophilic Residues</scene> are shown in purple. These residues prefer contact with water, and so typically appear on the surface of the protein |
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| + | <scene name='56/563219/Water_surrounding_enolase/1'>Water</scene> surrounding Enolase only reacts with the hydrophilic residues of the protein and forces the hydrophobic residues into the interior to minimize contact with them and so water can increase its own entropy. | ||
==Introduction== | ==Introduction== | ||
Revision as of 19:22, 9 October 2013
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| This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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More help: Help:Editing |
. This shows the alpha-helices in blue, and the beta-sheets in orange, as well as the non-repetitive structure in white
has lots of cool alpha-helices
is displayed here in red.
Because the beta-sheets are parallel, the H-bonds are not direct or straight, and therefore not as strong.
are shown in gray. These residues prefer little to no contact with water, and so typically hide in the interior of the protein
are shown in purple. These residues prefer contact with water, and so typically appear on the surface of the protein
surrounding Enolase only reacts with the hydrophilic residues of the protein and forces the hydrophobic residues into the interior to minimize contact with them and so water can increase its own entropy.
