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You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Function of your protein

The organism that Spy is from is Escherichia coli.The protein Spy can facilitate protein folding by allowing it to prevent clustering. That is done by grabbing the proteins as they start to misfold right before they are able to stick to other proteins to make big cluster. The protein also needs to bind very quickly.

Biological relevance and broader implications

There are diseases out there wondering if we can customize chaperons. One in particular is Alzheimer's because people with this disease could possibly have differences in their chaperons which could cause you to be more prone to that disease. You can be more prone because of the beta amyloid plaques being formed. By studying this protein and doing different experiments with it was helping to better understand how chaperons work.

Important amino acids

The protein Spy is one of those proteins that doesn't have a ligand. The ligand for Spy or any chaperon is proteins that are misfolding, so there isn't a specific ligand.

Structural highlights

The protein is 85% alpha helix, 10% beta sheet, and 5% other structures. The secondary structures show that the unfolding of substrates is preventing the protein to be clustered.

This shows how much space is being used in the protein and is also showing the quaternary feature.

This is showing how much hydrophobicity of the protein and positively charged.

Other important features

This shows where the amino acids are at that the protein is working with.

Most proteins are a ball shaped, but the protein Spy is a cradle shape because it is easier to attach to other proteins to properly allow folding.

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.