Premium
Protein‐Structure Prediction by Recombination of Fragments
Author(s) -
Bujnicki Janusz M.
Publication year - 2006
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500235
Subject(s) - protein structure prediction , computational biology , protein folding , homology modeling , protein design , protein structure , protein engineering , loop modeling , folding (dsp implementation) , protein evolution , computer science , biology , genetics , biochemistry , gene , engineering , electrical engineering , enzyme
The field of protein‐structure prediction has been revolutionized by the application of “mix‐and‐match” methods both in template‐based homology modeling and in template‐free de novo folding. Consensus analysis and recombination of fragments copied from known protein structures is currently the only approach that allows the building of models that are closer to the native structure of the target protein than the structure of its closest homologue. It is also the most successful approach in cases in which the target protein exhibits a novel three‐dimensional fold. This review summarizes the recent developments in both template‐based and template‐free protein structure modeling and compares the available methods for protein‐structure prediction by recombination of fragments. A convergence between the “protein folding” and “protein evolution” schools of thought is postulated.