Multicanonical chain-growth algorithm.
We present a temperature-independent Monte Carlo method for the determination of the density of states of lattice proteins that combines the fast ground-state search strategy of the new pruned-enriched Rosenbluth chain-growth method and multicanonical reweighting for sampling the complete energy space. Since the density of states contains all energetic information of a statistical system, we can directly calculate the mean energy, specific heat, Helmholtz free energy, and entropy for all temperatures. We apply this method to lattice proteins consisting of hydrophobic and polar monomers, and for the examples of sequences considered, we identify the transitions between native, globule, and random coil states. Since no special properties of heteropolymers are involved in this algorithm, the method applies to polymer models as well.
Bachmann
Michael
M
Institut für Theoretische Physik, Universität Leipzig, Augustusplatz 10/11, D-04109 Leipzig, Germany. michael.bachmann@itp.uni-leipzig.de
Janke
Wolfhard
W
D000465:Algorithms; D000596:Amino Acids / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D009010:Monte Carlo Method; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D000596:Amino Acids; D011506:Proteins