Literature DB >> 20205652

Why inverse proteins are relatively abundant.

Jean-Christophe Nebel1, Claude Godfrey Charles Walawage.   

Abstract

Studies have shown that inverse proteins are relatively abundant. In this work, we investigate the proposition that the repeat patterns they share with protein sequences explain this phenomenon. Using a new artificial set of peptide sequences which also display these features and a random set, we show that the presence of repeats contributes to protein sequence similarity. Further analysis confirms that most inverse proteins exhibit repeats. Therefore, we suggest the relative abundance of inverse proteins can be explained by the fact they display the same repeat structures and amino acid propensity of existing proteins.

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Year:  2010        PMID: 20205652     DOI: 10.2174/092986610791306698

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  2 in total

1.  Can natural proteins designed with 'inverted' peptide sequences adopt native-like protein folds?

Authors:  Settu Sridhar; Kunchur Guruprasad
Journal:  PLoS One       Date:  2014-09-11       Impact factor: 3.240

2.  Search and analysis of identical reverse octapeptides in unrelated proteins.

Authors:  Konda Mani Saravanan; Samuel Selvaraj
Journal:  Genomics Proteomics Bioinformatics       Date:  2013-03-21       Impact factor: 7.691

  2 in total

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