Identification of protein-protein interactions by mass spectrometry coupled techniques

Mohamed Abu-Farha, Fred Elisma, Daniel Figeys

Research output: Chapter in Book/Report/Conference proceedingChapter

14 Citations (Scopus)

Abstract

The use of mass spectrometry in protein identification has revolutionized the field of proteomics. Coupled to various affinity purification techniques, mass spectrometry is used to identify protein-protein interactions. This chapter looks at the use of these affinity purification techniques in the identification of protein interactions. Various tags are used to purify protein complexes including tandem affinity purification. The FLAG tag is another commonly used tag which is a small tag that tends not to interfere with the protein function. These different affinity purification methods are used to purify proteins that are further identified by either ESI-MS or MALDI-MS.

Original languageEnglish
Title of host publicationProtein - Protein Interaction
EditorsMeike Werther, Harald Seitz
Pages67-80
Number of pages14
DOIs
Publication statusPublished - 10 Sep 2008

Publication series

NameAdvances in Biochemical Engineering/Biotechnology
Volume110
ISSN (Print)0724-6145

Keywords

  • Affinity purification
  • Electrospray
  • Interactome
  • MALDI
  • Tandem affinity purification

Fingerprint Dive into the research topics of 'Identification of protein-protein interactions by mass spectrometry coupled techniques'. Together they form a unique fingerprint.

  • Cite this

    Abu-Farha, M., Elisma, F., & Figeys, D. (2008). Identification of protein-protein interactions by mass spectrometry coupled techniques. In M. Werther, & H. Seitz (Eds.), Protein - Protein Interaction (pp. 67-80). (Advances in Biochemical Engineering/Biotechnology; Vol. 110). https://doi.org/10.1007/10_2007_091