Quantification of proteins and their modifications using QconCAT technology

Kathleen M. Carroll, Francesco Lanucara, Claire E. Eyers

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review


Building a mathematical model of a biological system requires input of experimental data for each networked component, ultimately generating a model that can be used to test scientific hypotheses. A fundamental requirement in the computation of these systems is that the total amount of each component can be specified precisely. An added level of complexity occurs because a vast number of protein posttranslational modifications modulate protein function. Each of these modified forms therefore needs to be considered as a separate system component, and must therefore be quantified individually. In this chapter, we describe how designer QconCAT proteins can be used to determine the absolute amounts of both the polypeptide components and their covalently modified derivatives in both yeast and mammalian extracts derived from living cell populations. © 2011 Elsevier Inc. All rights reserved.
Original languageEnglish
Title of host publicationMethods in Enzymology
Subtitle of host publicationMethods in Systems Biology
EditorsDaniel Jameson, Malkhey Verma, Hans V. Westerhoff
Place of PublicationSan Diego
PublisherAcademic Press
Number of pages19
ISBN (Print)9780123851185
Publication statusPublished - 12 Nov 2011

Publication series

NameMethods in Enzymology
PublisherAcademic Press
ISSN (Print)0076-6879


  • isotope labelling
  • mass spectrometry
  • peptides
  • proteins
  • QconCAT
  • quantification
  • Trypsin


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