Protein Folding in the 2D HP Model

We study folding algorithms in the two-dimensional Hydrophobic- Hydrophilic model (2D HP model) for protein structure formation. We consider three generalizations of the best known approximation algorithm. We show that two of the generalizations do not improve the worst case approximation ratio. The third generalization seems to be better, and the analysis of its approximation ratio leads to an interesting combinatorial problem.

[1]  C. Anfinsen,et al.  The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. , 1961, Proceedings of the National Academy of Sciences of the United States of America.

[2]  K. Dill Theory for the folding and stability of globular proteins. , 1985, Biochemistry.

[3]  R Unger,et al.  Genetic algorithms for protein folding simulations. , 1992, Journal of molecular biology.

[4]  M. Karplus,et al.  How does a protein fold? , 1994, Nature.

[5]  William E. Hart,et al.  Fast protein folding in the hydrophobic-hydrophilic model within three-eights of optimal , 1995, STOC '95.

[6]  D. Yee,et al.  Principles of protein folding — A perspective from simple exact models , 1995, Protein science : a publication of the Protein Society.

[7]  K Yue,et al.  Forces of tertiary structural organization in globular proteins. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[8]  William E. Hart,et al.  Fast Protein Folding in the Hydrophobic-Hydrophillic Model within Three-Eights of Optimal , 1996, J. Comput. Biol..

[9]  B. Berger,et al.  Protein Folding in the Hydrophobic-Hydrophilic(HP) Model is NP-Complete , 1998, J. Comput. Biol..

[10]  Mihalis Yannakakis,et al.  On the Complexity of Protein Folding , 1998, J. Comput. Biol..

[11]  Giancarlo Mauri,et al.  Approximation algorithms for protein folding prediction , 1999, SODA '99.