Protein folding in the hydrophobic-hydrophilic (HP) is NP-complete
RECOMB '98 Proceedings of the second annual international conference on Computational molecular biology
On the complexity of protein folding (abstract)
RECOMB '98 Proceedings of the second annual international conference on Computational molecular biology
Constraint Techniques for Solving the Protein Structure Prediction Problem
CP '98 Proceedings of the 4th International Conference on Principles and Practice of Constraint Programming
Fast, Constraint-Based Threading of HP-Sequences to Hydrophobic Cores
CP '01 Proceedings of the 7th International Conference on Principles and Practice of Constraint Programming
Optimally Compact Finite Sphere Packings - Hydrophobic Cores in the FCC
CPM '01 Proceedings of the 12th Annual Symposium on Combinatorial Pattern Matching
Hi-index | 0.00 |
Lattice protein models are a major tool for investigating principles of protein folding. For this purpose, one needs an algorithm that is guaranteed to find the minimal energy conformation in some lattice model (at least for some sequences). So far, there are only algorithm that can find optimal conformations in the cubic lattice. In the more interesting case of the face-centered-cubic lattice (FCC), which is more protein-like, there are no results. One of the reasons is that for finding optimal conformations, one usually applies a branch-and-bound technique, and there are no reasonable bounds known for the FCC. We will give such a bound for Dill's HP-model on the FCC.