Abstract
Due to their different topologies, it is shown that the bulk and the interface contacts contribute differently to the folding mechanism of dimers. That is, the bulk displays a rich network of contacts, while pairs of residues belonging to different monomers interact independently of each other. This difference manifests itself in the different conservation patterns expected in the case of two-state and three-state dimers-conservation patterns that are the main point of contact between model predictions and real proteins.
| Original language | English |
|---|---|
| Article number | 051909 |
| Pages (from-to) | 051909/1-051909/9 |
| Journal | Physical Review E |
| Volume | 67 |
| Issue number | 5 1 |
| State | Published - May 2003 |
| Externally published | Yes |