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Successful recognition of protein folds using threading methods biased by sequence similarity and predicted secondary structure
Author(s) -
Jones David T.,
Tress Michael,
Bryson Kevin,
Hadley Caroline
Publication year - 1999
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(1999)37:3+<104::aid-prot14>3.0.co;2-p
Subject(s) - threading (protein sequence) , protein secondary structure , protein structure prediction , structural alignment , similarity (geometry) , pattern recognition (psychology) , sequence (biology) , artificial intelligence , protein structure , computational biology , computer science , biology , sequence alignment , crystallography , mathematics , peptide sequence , chemistry , genetics , biochemistry , image (mathematics) , gene
Analysis of our fold recognition results in the 3rd Critical Assessment in Structure Prediction (CASP3) experiment, using the programs THREADER 2 and GenTHREADER, shows an encouraging level of overall success. Of the 23 submitted predictions, 20 targets showed no clear sequence similarity to proteins of known 3D structure. These 20 targets can be divided into 22 domains, of which, 20 domains either entirely match a previously known fold, or partially match a substantial region of a known fold. Of these 20 domains, we correctly assigned the folds in 10 cases. Proteins Suppl 1999:3:104–111. © 1999 Wiley‐Liss, Inc.