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Tandem affinity purification combined with mass spectrometry to identify components of protein complexes


Meierhofer,  David
Mass Spectrometry (Head: David Meierhofer), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society;
Department of Biological Chemistry, College of Medicine, University of California Irvine, Irvine, CA, USA ;

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Kaiser, P., Meierhofer, D., Wang, X., & Huang, L. (2008). Tandem affinity purification combined with mass spectrometry to identify components of protein complexes. In M. Starkey, & R. Elaswarapu (Eds.), Methods in molecular biology (2nd edition, pp. 309-326). Humana Press.

Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-7EB1-2
Most biological processes are governed by multiprotein complexes rather than individual proteins. Identification of protein complexes therefore is becoming increasingly important to gain a molecular understanding of cells and organisms. Mass spectrometry—based proteomics combined with affinity-tag-based protein purification is one of the most effective strategies to isolate and identify protein complexes. The development of tandem-affinity purification approaches has revolutionized proteomics experiments. These two-step affinity purification strategies allow rapid, effective purification of protein complexes and, at the same time, minimize background. Identification of even very low-abundant protein complexes with modern sensitive mass spectrometers has become routine. Here, we describe two general strategies for tandem-affinity purification followed by mass spectrometric identification of protein complexes.