Folding and Design in Coarse-Grained Protein Models
Proceedings of the XVIIth International Symposium on Lattice Field Theory , eds. M. Campostrini et al., Nuclear Physics B (Proc. Suppl) 83-84, 712-714 (2000)
Recent advances in coarse-grained lattice and off-lattice protein models are reviewed. The sequence dependence of thermodynamical folding properties are investigated and evidence for non-randomness of the binary sequences of good folders are discussed. Similar patterns for non-randomness are found for real proteins. Dynamical parameter MC methods, such as the tempering and multisequence algorithms, are essential in order to obtain these results. Also, a new MC method for design, the inverse of folding, is presented. Here, one maximizes conditional probabilities rather than minimizing energies. By construction, this method ensures that the designed sequences represent good folders thermodynamically.
LU TP 99-25