@InProceedings{Backofen:Will:_const_based_approac_struc_predic:ICLP2003,
  author =	 {Rolf Backofen and Sebastian Will},
  title =	 {A Constraint-Based Approach to Structure Prediction
                  for Simplified Protein Models that Outperforms Other
                  Existing Methods},
  booktitle =	 {Proceedings of the 19th International Conference on
                  Logic Programming (ICLP 2003)},
  year =	 2003,
series     = {Lecture Notes in Computer Science},
volume     = 2916,
publisher  = {Springer}, 
  pages =        {49--71},
  user =	 {will},
  abstract =	 {Lattice protein models are used for hierarchical
                  approaches to protein structure prediction, as well
                  as for investigating general principles of protein
                  folding. So far, one has the problem that either the
                  lattice does not model real protein conformations
                  with good quality, or there is no efficient method
                  known for finding native conformations. We present a
                  constraint-based method that largely improves this
                  situ- ation. It outperforms all existing approaches
                  in lattice protein folding on the type of model we
                  have chosen (namely the HP-model by Lau and
                  Dill[34], which models the important aspect of
                  hydrophobicity). It is the only exact method that
                  has been applied to two different
                  lattices. Furthermore, it is the only exact method
                  for the face-centered cubic lattice. This lattice
                  is important since it has been shown [38] that the
                  FCC lattice can model real protein conformations
                  with coordinate root mean square deviation below 2
                  Angstrom. Our method uses a constraint-based approach. It
                  works by first calculating maximally compact sets
                  of points (hydrophobic cores), and then threading
                  the given HP-sequence to the hydrophobic cores such
                  that the core is occupied by H-monomers.}
}