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

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

5 Scopus citations


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 languageAmerican English
Title of host publicationSelenium
Subtitle of host publicationIts Molecular Biology and Role in Human Health, Fourth Edition
PublisherSpringer International Publishing
Number of pages11
ISBN (Electronic)9783319412832
ISBN (Print)9783319412818
StatePublished - 1 Jan 2016

Bibliographical note

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


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


Dive into the research topics of 'The chemistry of selenocysteine in proteins'. Together they form a unique fingerprint.

Cite this