Literature DB >> 17894329

Fams-ace: a combined method to select the best model after remodeling all server models.

Genki Terashi1, Mayuko Takeda-Shitaka, Kazuhiko Kanou, Mitsuo Iwadate, Daisuke Takaya, Akio Hosoi, Kazuhiro Ohta, Hideaki Umeyama.   

Abstract

During Critical Assessment of Protein Structure Prediction (CASP7, Pacific Grove, CA, 2006), fams-ace was entered in the 3D coordinate prediction category as a human expert group. The procedure can be summarized by the following three steps. (1) All the server models were refined and rebuilt utilizing our homology modeling method. (2) Representative structures were selected from each server, according to a model quality evaluation, based on a 3D1D profile score (like Verify3D). (3) The top five models were selected and submitted in the order of the consensus-based score (like 3D-Jury). Fams-ace is a fully automated server and does not require human intervention. In this article, we introduce the methodology of fams-ace and discuss the successes and failures of this approach during CASP7. In addition, we discuss possible improvements for the next CASP. (c) 2007 Wiley-Liss, Inc.

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Year:  2007        PMID: 17894329     DOI: 10.1002/prot.21785

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  10 in total

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Journal:  Proteins       Date:  2008-08-15

8.  Alternating evolutionary pressure in a genetic algorithm facilitates protein model selection.

Authors:  Marc N Offman; Alexander L Tournier; Paul A Bates
Journal:  BMC Struct Biol       Date:  2008-08-01

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Authors:  Yosuke Amagai; Akira Matsuda; Kyungsook Jung; Kumiko Oida; Hyosun Jang; Saori Ishizaka; Hiroshi Matsuda; Akane Tanaka
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10.  SP5: improving protein fold recognition by using torsion angle profiles and profile-based gap penalty model.

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Journal:  PLoS One       Date:  2008-06-04       Impact factor: 3.240

  10 in total

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