Improving mass defect filters for human proteins

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Issue Date
2010-10-01Author
Toumi, Melinda L.
Desaire, Heather
Publisher
American Chemical Society
Type
Article
Article Version
Scholarly/refereed, author accepted manuscript
Rights
This document is the Accepted Manuscript version of a Published Work that appeared in final form in the Journal of Proteome Research, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/pr100291q.
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Show full item recordAbstract
The mass defect of a substance can be used in mass spectral analysis to identify peaks as likely belonging to a compound class, such as peptides, if the mass defect is within the known range for that compound class. For peptides, a range of possible mass defects was calculated previously, using a set of theoretical peptides, where all possible amino acid combinations were considered (Mann, M. Abstract from the 43rd Annual Conference on Mass Spectrometry and Allied Topics; 1995, ASMS). We compare that range of theoretical peptide mass defects to new values obtained from in silico tryptic digests of proteins that are abundant in human serum and human seminal fluid. The range of mass defect values encompassing 95% of peptides for the human protein data sets was found to be up to 50% smaller than the previously reported mass defect range for the theoretical peptides. The smaller range established for human tryptic peptides can be used to improve peptide mass defect filters by excluding more species that are not likely to be peptides, thus improving filter selectivity for peptides during proteomic data analysis.
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Citation
Toumi, M. L., & Desaire, H. (2010). Improving mass defect filters for human proteins. Journal of Proteome Research, 9(10), 5492–5495. http://doi.org/10.1021/pr100291q
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