Title |
On the amyloid datasets used for training PAFIG how (not) to extend the experimental dataset of hexapeptides
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Published in |
BMC Bioinformatics, December 2013
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DOI | 10.1186/1471-2105-14-351 |
Pubmed ID | |
Authors |
Malgorzata Kotulska, Olgierd Unold |
Abstract |
Amyloids are proteins capable of forming aberrant intramolecular contact sites, characteristic of beta zipper configuration. Amyloids can underlie serious health conditions, e.g. Alzheimer's or Parkinson's diseases. It has been proposed that short segments of amino acids can be responsible for protein amyloidogenicity, but no more than two hundred such hexapeptides have been experimentally found. The authors of the computational tool Pafig published in BMC Bioinformatics a method for extending the amyloid hexapeptide dataset that could be used for training and testing models. They assumed that all hexapeptides belonging to an amyloid protein can be regarded as amylopositive, while those from proteins never reported as amyloid are always amylonegative. Here we show why the above described method of extending datasets is wrong and discuss the reasons why the incorrect data could lead to falsely correct classification. |
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