Folding and Design in Coarse-Grained Protein Models

Details Folding and Design in Coarse-Grained Protein Models Folding and Design in Coarse-Grained Protein Models

1999-09-02

arxiv.org/abs/hep-lat/9909015v1

Nucl.Phys.Proc.Suppl. 83 (2000) 712-714

Physics

High Energy Physics

High Energy Physics - Lattice

LATTICE 99 (Spin Models), 3 pages, 1 figure, espcrc2.sty

Scientific paper

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.

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