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Updated: Jun 23, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
Published on: June 19, 2010
New dimensions in the study of protein complexes using quantitative mass spectrometry
Silke Oeljeklaus1, Helmut E Meyer, Bettina Warscheid
1Medizinisches Proteom-Center, Zentrum fuer klinische Forschung, Ruhr-Universitaet Bochum, Universitaetsstrasse 150, 44780 Bochum, Germany.
Abstract:
Mass spectrometry combined with affinity purification techniques has evolved as a prime tool for the in-depth study of distinct protein complexes and protein-protein interactions. It fueled proteome-wide studies leading to the establishment of intricate cellular protein interaction networks. Recent innovative advancements in quantitative protein mass spectrometry act as driving force for the design of ingenious strategies in interaction proteomics facilitating the acquisition of interaction data with improved accuracy and, most intriguingly, the elucidation of functional aspects by monitoring transient interactions as well as dynamic changes in composition, stoichiometry, localization and post-translational modification of protein complexes under various conditions.
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