Toy model for protein folding
Abstract
A conceptually simple model for protein-folding phenomena has been created: it is two-dimensional and has only two different ``amino acids.'' Ground-state conformations have been determined for all of its flexible polypeptides containing seven or fewer monomers. This complete database displays a wide geometric variety of folded shapes and shows that single point mutations in some cases induce substantial folding modifications. Neural-network concepts have been employed to analyze results. The simplest static neural networks required to act as error-free read-only memories provide a way to visualize the logical structure of underlying folding principles. The topologies of optimal networks found thus far suggest that protein folding has a more complex cooperative character than has been embodied previously in theoretical approaches.
- Publication:
-
Physical Review E
- Pub Date:
- August 1993
- DOI:
- 10.1103/PhysRevE.48.1469
- Bibcode:
- 1993PhRvE..48.1469S
- Keywords:
-
- 87.10.+e;
- 87.15.By;
- 42.79.Ta;
- General theory and mathematical aspects;
- Structure and bonding;
- Optical computers logic elements interconnects switches;
- neural networks