title: Protein model refinement using structural fragment tessellation.
abstract: A method is described for the refinement of rough protein models based on finding a selection of structural fragments that match the model. Unlike most fragment-based methods, these are not necessarily contiguous in the sequence and form a tiling (tessellation) that covers most of the structure. The residue positions of the fragments are then used as a target for the model atoms to generate a revised model which is used as the basis of a subsequent pattern definition and search. The method was shown to improve the recognition of the native fold in a series of decoys largely as a result of improved secondary structure representation.
authors.affiliation: Computational Biology Unit and Department of Informatics, University of Bergen, Norway.
authors.forename: Inge
authors.initials: I
authors.lastname: Jonassen
authors.forename: Daniel
authors.initials: D
authors.lastname: Klose
authors.forename: William R
authors.initials: WR
authors.lastname: Taylor
mesh_terms: D000465:Algorithms; D003198:Computer Simulation; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins