Abstract
While the existence of the rare 21st proteinogenic amino acid, selenocysteine (Sec, U) in cellular proteins has been known for over 40 years, recent advances in peptide chemistry have supported its importance not only in the biological function of natural selenoproteins, but also in synthetic systems. Besides its obvious applications in the synthesis of selenoproteins, fundamental differences between the chemistry of cysteine’s thiol and Sec’s selenol moieties have added a surprising number of technologies to the protein chemist’s toolbox. In this chapter, we discuss Sec’s impact on chemical protein synthesis, folding of challenging disulfide-rich proteins, and the chemistry of the little-understood selenoproteins, SEP15 and SELM. Additional important aspects on Sec will be the subjects of other chapters in this book.
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Acknowledgements
Research in our group is supported by Maof fellowship, Israel Science Foundation (1072/14), the US-Israel Bi-national Science Foundation (BSF) (2014167), the Lejwa Fund for Biochemistry and the German-Israeli Foundation for Scientific Research and Development (GIF) (I-2340-302.5/2014). P.S.R. is supported by the PBC fellowship, Council for Higher Education, Israel. RND is supported by the Kaete Klausner fellowship.
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Dardashti, R.N., Dery, L., Mousa, R., Dery, S., Reddy, P.S., Metanis, N. (2016). The Chemistry of Selenocysteine in Proteins. In: Hatfield, D., Schweizer, U., Tsuji, P., Gladyshev, V. (eds) Selenium. Springer, Cham. https://doi.org/10.1007/978-3-319-41283-2_7
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DOI: https://doi.org/10.1007/978-3-319-41283-2_7
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