4.5 Article Proceedings Paper

New dimensions in the study of protein complexes using quantitative mass spectrometry

期刊

FEBS LETTERS
卷 583, 期 11, 页码 1674-1683

出版社

WILEY
DOI: 10.1016/j.febslet.2009.04.018

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Affinity purification; Quantitative mass spectrometry; Protein complex; Protein-protein interaction; Dynamics; Stoichiometry

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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. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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