Literature DB >> 22956349

A simple recipe for the non-expert bioinformaticist for building experimentally-testable hypotheses for proteins with no known homologs.

Alexander Zawaira1, Youtaro Shibayama.   

Abstract

The study of the protein-protein interactions (PPIs) of unique ORFs is a strategy for deciphering the biological roles of unique ORFs of interest. For uniform reference, we define unique ORFs as those for which no matching protein is found after PDB-BLAST search with default parameters. The uniqueness of the ORFs generally precludes the straightforward use of structure-based approaches in the design of experiments to explore PPIs. Many open-source bioinformatics tools, from the commonly-used to the relatively esoteric, have been built and validated to perform analyses and/or predictions of sorts on proteins. How can these available tools be combined into a protocol that helps the non-expert bioinformaticist researcher to design experiments to explore the PPIs of their unique ORF? Here we define a pragmatic protocol based on accessibility of software to achieve this and we make it concrete by applying it on two proteins-the ImuB and ImuA' proteins from Mycobacterium tuberculosis. The protocol is pragmatic in that decisions are made largely based on the availability of easy-to-use freeware. We define the following basic and user-friendly software pathway to build testable PPI hypotheses for a query protein sequence: PSI-PRED → MUSTER → metaPPISP → ASAView and ConSurf. Where possible, other analytical and/or predictive tools may be included. Our protocol combines the software predictions and analyses with general bioinformatics principles to arrive at consensus, prioritised and testable PPI hypotheses.

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Year:  2012        PMID: 22956349     DOI: 10.1007/s10969-012-9141-7

Source DB:  PubMed          Journal:  J Struct Funct Genomics        ISSN: 1345-711X


  79 in total

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Authors:  Alice Douangamath; Fabian V Filipp; André T J Klein; Phil Barnett; Peijian Zou; Tineke Voorn-Brouwer; M Cristina Vega; Olga M Mayans; Michael Sattler; Ben Distel; Matthias Wilmanns
Journal:  Mol Cell       Date:  2002-11       Impact factor: 17.970

Review 4.  Fold recognition methods.

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Journal:  Methods Biochem Anal       Date:  2003

5.  HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment.

Authors:  Michael Remmert; Andreas Biegert; Andreas Hauser; Johannes Söding
Journal:  Nat Methods       Date:  2011-12-25       Impact factor: 28.547

6.  Protein structure prediction on the Web: a case study using the Phyre server.

Authors:  Lawrence A Kelley; Michael J E Sternberg
Journal:  Nat Protoc       Date:  2009       Impact factor: 13.491

7.  Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures.

Authors:  Zhucheng Chen; Haijuan Yang; Nikola P Pavletich
Journal:  Nature       Date:  2008-05-22       Impact factor: 49.962

8.  An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.

Authors:  L Holm; C Sander
Journal:  Proteins       Date:  1997-05

9.  ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures.

Authors:  Meytal Landau; Itay Mayrose; Yossi Rosenberg; Fabian Glaser; Eric Martz; Tal Pupko; Nir Ben-Tal
Journal:  Nucleic Acids Res       Date:  2005-07-01       Impact factor: 16.971

10.  'Double water exclusion': a hypothesis refining the O-ring theory for the hot spots at protein interfaces.

Authors:  Jinyan Li; Qian Liu
Journal:  Bioinformatics       Date:  2009-01-29       Impact factor: 6.937

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