Abstract
Proteome solubility contains latent information on the nature of protein interaction networks in cells and changes in solubility can provide information on rewiring of networks. Here, we report a simple one-step ultracentrifugation method to separate the soluble and insoluble fraction of the proteome. The method involves quantitative proteomics and a bioinformatics strategy to analyze the changes that arise. Because protein solubility changes are also associated with protein misfolding and aggregation in neurodegenerative disease, we also include a protocol for isolating disease-associated protein aggregates with pulse shape analysis (PulSA) by flow cytometry as a complementary approach that can be used alongside the more general measure of solubility or as a stand-alone approach.
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Sui, X., Radwan, M., Cox, D., Hatters, D.M. (2022). Probing Protein Solubility Patterns with Proteomics for Insight into Network Dynamics. In: Matějů, D., Chao, J.A. (eds) The Integrated Stress Response. Methods in Molecular Biology, vol 2428. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1975-9_16
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DOI: https://doi.org/10.1007/978-1-0716-1975-9_16
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