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Journal Article
Analysis of protein complexes using mass spectrometry
2007
Overview
Key Points
In this article, we review the current status of affinity purification and mass spectrometry (AP–MS) and its promise for better understanding protein complexes, complex structure and the dynamics of complex formation.
We describe the general AP–MS strategy, with an emphasis on generic approaches (flag-tag, tandem AP) and how AP–MS of multiple components (that is, high-density AP–MS) can help to reveal the true composition of protein complexes.
Recent high-throughput studies with flag-tagging or tandem AP significantly improved our understanding of protein–protein interactions in yeast.
AP–MS can be combined with classical biochemical purification approaches to reveal complex composition and to resolve the problem of mutually exclusive complexes co-precipitating with the same tagged protein.
Crosslinkers can contribute to AP–MS strategies by stabilizing weak or transient protein interactions and by revealing details concerning complex organization and interacting surfaces.
Stoichiometry of protein complexes can be obtained using intact-complex mass measurement and absolute quantitative proteomics tools.
Quantitative proteomics approaches can help to decipher the dynamics of protein-complex formation.
The combination of affinity purification and mass spectrometry (AP–MS) has recently been applied to the detailed characterization of protein complexes and large protein-interaction networks. Emerging AP–MS approaches promise a better understanding of protein-complex stoichiometry, structural organization and the dynamics of protein-complex composition.
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group
