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Detection of Heterogeneous Protein S-Acylation in Cells

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Protein Lipidation

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2009))

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Abstract

The use of synthetically synthesized azide and alkyne fatty acid analogs coupled with bioorthogonal Cu(i)-catalyzed Huisgen 1,3-dipolar cycloaddition reaction-based detection methods to study protein S-acylation reactions has replaced the traditional method of using in vivo metabolic radiolabeling with tritiated palmitic acid and has greatly facilitated our understanding of this essential cellular process. Here, we describe the chemical synthesis of myristic (C:14), palmitic (C16:0), and stearic (C18:0) acid-azide probes and detail how they may be utilized as chemical reporters for the analysis of S-acylation of exogenously expressed proteins in cells.

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Correspondence to Jennifer Greaves .

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Greaves, J., Tomkinson, N.C.O. (2019). Detection of Heterogeneous Protein S-Acylation in Cells. In: Linder, M. (eds) Protein Lipidation. Methods in Molecular Biology, vol 2009. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9532-5_2

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  • DOI: https://doi.org/10.1007/978-1-4939-9532-5_2

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-4939-9531-8

  • Online ISBN: 978-1-4939-9532-5

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