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We have subjected several sets of real and simplified model proteins to Delaunay tessellation and have computed statistics on both Delaunay simplex geometry and the tendency of quadruplets of residue types to be joined together in simplices. We have characterized the geometry and contact patterns of real proteins and some of the ways in which they differ from these model structures. We have also found...
We describe a fully automated method of protein structural domain assignment using a Potts model which we call DePot (an abbreviation for Delaunay- Potts). It is a heavily modified version of a method described previously by WR Taylor. Each amino acid residue is represented as a site in an irregular lattice derived from the Delaunay tessellation of the protein structure. Domain membership is represented...
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