Dynamical-Parameter Algorithms for Protein Folding

نویسنده

  • Anders Irbäck
چکیده

Two different dynamical-parameter algortihms are discussed, simulated tempering and the multisequence method. Using simulated tempering, the folding properties of 300 random sequences in a simple off-lattice model with only two amino-acid types, hydrophobic and hydrophilic, are investigated. A careful statistical analysis shows that the hydrophobic monomers are anticorrelated along the chains for good folding sequences. The multisequence method is the basis for a novel procedure for maximizing the stability of a given target structure. Tests of this sequence design procedure on the HP lattice model show that it can be extremely efficient.

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تاریخ انتشار 1998