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Review

Complexome Profiling: Assembly and Remodeling of Protein Complexes

Institute for Cardiovascular Physiology, Goethe University, 60590 Frankfurt, Germany
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Author to whom correspondence should be addressed.
Academic Editor: Christof Lenz
Int. J. Mol. Sci. 2021, 22(15), 7809; https://doi.org/10.3390/ijms22157809
Received: 13 June 2021 / Revised: 13 July 2021 / Accepted: 19 July 2021 / Published: 21 July 2021
Many proteins have been found to operate in a complex with various biomolecules such as proteins, nucleic acids, carbohydrates, or lipids. Protein complexes can be transient, stable or dynamic and their association is controlled under variable cellular conditions. Complexome profiling is a recently developed mass spectrometry-based method that combines mild separation techniques, native gel electrophoresis, and density gradient centrifugation with quantitative mass spectrometry to generate inventories of protein assemblies within a cell or subcellular fraction. This review summarizes applications of complexome profiling with respect to assembly ranging from single subunits to large macromolecular complexes, as well as their stability, and remodeling in health and disease. View Full-Text
Keywords: complexome profiling; mass spectrometry; protein complexes; protein–protein interaction; assembly; remodeling; data repositories complexome profiling; mass spectrometry; protein complexes; protein–protein interaction; assembly; remodeling; data repositories
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MDPI and ACS Style

Wittig, I.; Malacarne, P.F. Complexome Profiling: Assembly and Remodeling of Protein Complexes. Int. J. Mol. Sci. 2021, 22, 7809. https://doi.org/10.3390/ijms22157809

AMA Style

Wittig I, Malacarne PF. Complexome Profiling: Assembly and Remodeling of Protein Complexes. International Journal of Molecular Sciences. 2021; 22(15):7809. https://doi.org/10.3390/ijms22157809

Chicago/Turabian Style

Wittig, Ilka, and Pedro F. Malacarne 2021. "Complexome Profiling: Assembly and Remodeling of Protein Complexes" International Journal of Molecular Sciences 22, no. 15: 7809. https://doi.org/10.3390/ijms22157809

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