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Heteromer score—using internal standards to assess the quality of proteomic data

Authors

  • Adelina Rogowska-Wrzesinska,

    1. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark
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  • Krzysztof Wrzesinski,

    1. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark
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  • Stephen J. Fey

    Corresponding author
    1. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark
    • Correspondence: Dr. Stephen J. Fey, Department of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense M, Denmark

      E-mail: sjf@bmb.sdu.dk

      Fax: +45-6550-2467

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Abstract

In the cell, the majority of proteins exist in complexes. Most of these complexes have a constant stoichiometry and thus can be used as internal standards. In this rapid communication, we show that it is possible to calculate a correlation coefficient that reflects the reproducibility of the analytical approach used. The abundance of one subunit in a heterodimer is plotted against the abundance of the other, and this is repeated for all subunits in all heteromers found in the data set. The correlation coefficient obtained (the “heteromer score”) is a new bioinformatic tool that is independent of the method used to collect the data, requires no special sample preparation and can be used retrospectively on old datasets. It can be used for quality control, to indicate when a change becomes significant or identify complexes whose stoichiometry has been perturbed during the experiment.

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