| Original View | |
| Make the atoms transparent to reveal the skeleton of the molecule. | |
| Remove the sidechains to see the sheet structure more clearly. | |
| Play a short movie to see the hydrogen bonds stabilizing the helix. In the movie, oxygen and nitrogen atoms involved in h-bonding pop out as red and blue spheres, respectively. | |
| Rebuild the molecule |
| This sheet forms a part of a larger protein. In this presentation, the rest of the protein is not shown so that you can see the sheet structure more clearly. However, you can see how the sheet might interact with the rest of the protein by looking for the hydrophobic and hydrophilic sidechains. |
| See hydrophobic sidechains in green |
| Note the concentration of hydrophobic sidechains in one spot on one side of the sheet. |
| See hydrophilic sidchains in blue |
| Proteins fold so as to minimize the contact of hyrophobic sidechains with their aqueous environment. If this sheet were restored to its original protein, which face of the sheet would you expect to be buried? Which face will be in contact with solvent? |
| Back to Alpha-Helix |