| Literature DB >> 28028736 |
Tambi Richa1, Soichiro Ide1, Ryosuke Suzuki1, Teppei Ebina1,2, Yutaka Kuroda3.
Abstract
Efficient and rapid prediction of domain regions from amino acid sequence information alone is often required for swift structural and functional characterization of large multi-domain proteins. Here we introduce Fast H-DROP, a thirty times accelerated version of our previously reported H-DROP (Helical Domain linker pRediction using OPtimal features), which is unique in specifically predicting helical domain linkers (boundaries). Fast H-DROP, analogously to H-DROP, uses optimum features selected from a set of 3000 ones by combining a random forest and a stepwise feature selection protocol. We reduced the computational time from 8.5 min per sequence in H-DROP to 14 s per sequence in Fast H-DROP on an 8 Xeon processor Linux server by using SWISS-PROT instead of Genbank non-redundant (nr) database for generating the PSSMs. The sensitivity and precision of Fast H-DROP assessed by cross-validation were 33.7 and 36.2%, which were merely ~2% lower than that of H-DROP. The reduced computational time of Fast H-DROP, without affecting prediction performances, makes it more interactive and user-friendly. Fast H-DROP and H-DROP are freely available from http://domserv.lab.tuat.ac.jp/ .Keywords: Optimum features; PSSM; Random forest; Stepwise selection
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Year: 2016 PMID: 28028736 DOI: 10.1007/s10822-016-9999-8
Source DB: PubMed Journal: J Comput Aided Mol Des ISSN: 0920-654X Impact factor: 3.686