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.
CITATION STYLE
Greaves, J., & Tomkinson, N. C. O. (2019). Detection of heterogeneous protein S-acylation in cells. In Methods in Molecular Biology (Vol. 2009, pp. 13–33). Humana Press Inc. https://doi.org/10.1007/978-1-4939-9532-5_2
Mendeley helps you to discover research relevant for your work.