Sandbox Reserved 807
From Proteopedia
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<scene name='56/563219/Hydrogen_bonding_in_backbone/1'>Hydrogen Bonding</scene> is displayed here in red. | <scene name='56/563219/Hydrogen_bonding_in_backbone/1'>Hydrogen Bonding</scene> is displayed here in red. | ||
| - | <scene name='56/563219/H-bonding_between_beta-sheets/1'>H-bonds in beta-sheets</scene> are not direct or straight, and therefore not as strong | + | <scene name='56/563219/H-bonding_between_beta-sheets/1'>H-bonds in beta-sheets</scene> Because the beta-sheets are parallel, the H-bonds are not direct or straight, and therefore not as strong. |
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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 | ||
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| + | <scene name='56/563219/Hydrophilic_residues/1'>Hydrophillic Residues</scene> are shown in purple. These residues prefer contact with water, and so typically appear on the surface of the protein | ||
==Introduction== | ==Introduction== | ||
Revision as of 19:10, 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. |
To get started:
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
