The chemistry of selenocysteine in proteins

Rebecca N. Dardashti; Linoy Dery; Reem Mousa; Shahar Dery; Post S. Reddy; Norman Metanis

doi:10.1007/978-3-319-41283-2_7

The chemistry of selenocysteine in proteins

Rebecca N. Dardashti, Linoy Dery, Reem Mousa, Shahar Dery, Post S. Reddy, Norman Metanis^*

^*Corresponding author for this work

Institute of Chemistry

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

5 Scopus citations

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.

Original language	English
Title of host publication	Selenium
Subtitle of host publication	Its Molecular Biology and Role in Human Health, Fourth Edition
Publisher	Springer International Publishing
Pages	73-83
Number of pages	11
ISBN (Electronic)	9783319412832
ISBN (Print)	9783319412818
DOIs	https://doi.org/10.1007/978-3-319-41283-2_7
State	Published - 1 Jan 2016

Bibliographical note

Publisher Copyright:
© Springer Science+Business Media, LLC 2001, 2006, 2012, 2016.

Keywords

Chemical protein synthesis
Deselenization
Desulfurization
Native chemical ligation
Oxidative protein folding
Selenocysteine
Selenoproteins

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10.1007/978-3-319-41283-2_7

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AU - Reddy, Post S.

AU - Metanis, Norman

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AB - 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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KW - Desulfurization

KW - Native chemical ligation

KW - Oxidative protein folding

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The chemistry of selenocysteine in proteins

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Keywords

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