Abstract

The versatile combination of affinity purification and mass spectrometry (AP–MS) has recently been applied to the detailed characterization of many protein complexes and large protein-interaction networks. The combination of AP–MS with other techniques, such as biochemical fractionation, intact mass measurement and chemical crosslinking, can help to decipher the supramolecular organization of protein complexes. AP–MS can also be combined with quantitative proteomics approaches to better understand the dynamics of protein–complex assembly.

Author affiliations

1. Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Ave, Room 992A, Toronto, Ontario, M5G 1X5, Canada; and Department of Medical & Molecular Genetics and Graduate Department of Molecular & Medical Genetics, University of Toronto, Toronto, Canada.
2. Institute of Molecular Systems Biology, Swiss Federal Institute of Technology, ETH Hönggerberg HPT E 78, CH-8093 Zürich, Switzerland; and Competence Center for Systems Physiology and Metabolic Diseases, Zurich, Switzerland.
3. University Health Network, Ontario Cancer Institute and McLaughlin Centre for Molecular Medicine, 101 College St, MaRS TMDT 9-805, Toronto, Ontario, M5G 1L7, Canada; and Department of Medical Biophysics, University of Toronto, Toronto, Canada.
4. Institute for Systems Biology, 1441 N. 34th St, Seattle, Washington 98103, USA; and Faculty of Science, University of Zurich, Switzerland.

Correspondence to: Anne-Claude Gingras¹ Email: gingras@mshri.on.ca

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