What is it about?
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 is called the “heteromer score”.
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Why is it important?
This approach - to use biological 'structures to indicate data quality can be used with any method that quantitiatively measures protein abundance. There are many complexes in the cell and thus proteins can act as internal standards to control for protein degradation, differential extraction or detection.
Perspectives
This paper provides an easy double check on technical processes involved in protein research. Deviations from the expected heteromer ratio could indicate novel functionality of one or more subunits.
Professor Stephen John Fey
CelVivo
Read the Original
This page is a summary of: Heteromer score-using internal standards to assess the quality of proteomic data, PROTEOMICS, April 2014, Wiley,
DOI: 10.1002/pmic.201300457.
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