title: Identification of protein-protein interactions by mass spectrometry coupled techniques.
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.
authors.affiliation: Ottawa Institute of Systems Biology (OISB), University of Ottawa, 451 Smyth Road. Ottawa, K1H 8M5, Ontario, Canada.
authors.forename: Mohamed
authors.initials: M
authors.lastname: Abu-Farha
authors.forename: Fred
authors.initials: F
authors.lastname: Elisma
authors.forename: Daniel
authors.initials: D
authors.lastname: Figeys
mesh_terms: D000345:Affinity Labels; D013058:Mass Spectrometry / Q000379:methods*; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000378:metabolism*
chemical_list: D000345:Affinity Labels; D011506:Proteins