Protein model refinement using structural fragment tessellation.
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.
Jonassen
Inge
I
Computational Biology Unit and Department of Informatics, University of Bergen, Norway.
Klose
Daniel
D
Taylor
William R
WR
D000465:Algorithms; D003198:Computer Simulation; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
D011506:Proteins