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Search for the most stable folds of protein chains: III. Improvement in fold recognition by averaging over homologous sequences and 3D structures
Author(s) -
Rykunov D.S.,
Lobanov M.Yu.,
Finkelstein A.V.
Publication year - 2000
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 - 10.1002/1097-0134(20000815)40:3<494::aid-prot160>3.0.co;2-#
Subject(s) - threading (protein sequence) , homologous chromosome , fold (higher order function) , protein superfamily , computational biology , sequence (biology) , computer science , protein structure , biology , pattern recognition (psychology) , genetics , artificial intelligence , gene , biochemistry , programming language
Three‐dimensional (3D) protein fold recognition by query sequence can be improved using information of fold recognition yielded by the sequences homologous to the query one. This idea is now used more and more widely. Our paper presents its consequent development. We suggest incorporating information both on the sequences homologous to the query protein sequence and the 3D structures homologous to the target (already deciphered) protein folds. We show that both these tricks, and especially their combination reduces errors in fold recognition by the threading method. Proteins 2000;40:494–501. © 2000 Wiley‐Liss, Inc.