Understanding protein interactions within the complexity of a living cell is challenging, but techniques coupling affinity purification and mass spectrometry have enabled important progress to be made in the past 15 years. As identification of protein-protein interactions is becoming easier, the quantification of the interaction dynamics is the next frontier. Several quantitative mass spectrometric approaches have been developed to address this issue that vary in their strengths and weaknesses. While isotopic labeling approaches continue to contribute to the identification of regulated interactions, techniques that do not require labeling are becoming increasingly used in the field. Here, we describe the major types of label-free quantification used in interaction proteomics, and discuss the relative merits of data dependent and data independent acquisition approaches in label-free quantification. This article is part of a Special Issue entitled: From protein structures to clinical applications.
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