Literature DB >> 15498561

Reduced amino acid alphabet is sufficient to accurately recognize intrinsically disordered protein.

Edward A Weathers1, Michael E Paulaitis, Thomas B Woolf, Jan H Hoh.   

Abstract

Intrinsically disordered proteins are an important class of proteins with unique functions and properties. Here, we have applied a support vector machine (SVM) trained on naturally occurring disordered and ordered proteins to examine the contribution of various parameters (vectors) to recognizing proteins that contain disordered regions. We find that a SVM that incorporates only amino acid composition has a recognition accuracy of 87+/-2%. This result suggests that composition alone is sufficient to accurately recognize disorder. Interestingly, SVMs using reduced sets of amino acids based on chemical similarity preserve high recognition accuracy. A set as small as four retains an accuracy of 84+/-2%; this suggests that general physicochemical properties rather than specific amino acids are important factors contributing to protein disorder.

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Year:  2004        PMID: 15498561     DOI: 10.1016/j.febslet.2004.09.036

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  43 in total

1.  Net charge per residue modulates conformational ensembles of intrinsically disordered proteins.

Authors:  Albert H Mao; Scott L Crick; Andreas Vitalis; Caitlin L Chicoine; Rohit V Pappu
Journal:  Proc Natl Acad Sci U S A       Date:  2010-04-19       Impact factor: 11.205

Review 2.  Understanding protein non-folding.

Authors:  Vladimir N Uversky; A Keith Dunker
Journal:  Biochim Biophys Acta       Date:  2010-02-01

Review 3.  Computational prediction of type III and IV secreted effectors in gram-negative bacteria.

Authors:  Jason E McDermott; Abigail Corrigan; Elena Peterson; Christopher Oehmen; George Niemann; Eric D Cambronne; Danna Sharp; Joshua N Adkins; Ram Samudrala; Fred Heffron
Journal:  Infect Immun       Date:  2010-10-25       Impact factor: 3.441

4.  Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions.

Authors:  Jessica Walton Chen; Pedro Romero; Vladimir N Uversky; A Keith Dunker
Journal:  J Proteome Res       Date:  2006-04       Impact factor: 4.466

5.  Studies on titin PEVK peptides and their interaction.

Authors:  Yingli Duan; Joshua G DeKeyser; Srinivasan Damodaran; Marion L Greaser
Journal:  Arch Biochem Biophys       Date:  2006-08-15       Impact factor: 4.013

Review 6.  Protein aggregation processes: In search of the mechanism.

Authors:  Carl Frieden
Journal:  Protein Sci       Date:  2007-11       Impact factor: 6.725

Review 7.  On the key role played by altered protein conformation in Parkinson's disease.

Authors:  L F Agnati; E Baldelli; N Andreoli; A S Woods; V Vellani; D Marcellino; D Guidolin; K Fuxe
Journal:  J Neural Transm (Vienna)       Date:  2008-06-05       Impact factor: 3.575

8.  Polycomb group protein Suppressor 2 of zeste is a functional homolog of Posterior Sex Combs.

Authors:  Stanley M Lo; Nitin K Ahuja; Nicole J Francis
Journal:  Mol Cell Biol       Date:  2008-11-03       Impact factor: 4.272

Review 9.  Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins.

Authors:  Deepa Balasubramaniam; Elizabeth A Komives
Journal:  Biochim Biophys Acta       Date:  2012-10-22

Review 10.  Describing sequence-ensemble relationships for intrinsically disordered proteins.

Authors:  Albert H Mao; Nicholas Lyle; Rohit V Pappu
Journal:  Biochem J       Date:  2013-01-15       Impact factor: 3.857

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