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  Amino acid chalcogen analogues as tools in peptide and protein research

Moroder, L., & Musiol, H.-J. (2020). Amino acid chalcogen analogues as tools in peptide and protein research. JOURNAL OF PEPTIDE SCIENCE, 26(2): e3232. doi:10.1002/psc.3232.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-A122-E Version Permalink: http://hdl.handle.net/21.11116/0000-0005-AF24-E
Genre: Journal Article
Other : Review

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 Creators:
Moroder, Luis1, Author              
Musiol, Hans-Jürgen1, Author              
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1Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              

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Free keywords: DISULFIDE INTERCHANGE REACTIONS; SELENIUM-CONTAINING PHYCOCYANIN; IN-VITRO ANTIOXIDANT; X-RAY-STRUCTURE; ESCHERICHIA-COLI; PRION PROTEIN; THIOREDOXIN REDUCTASE; ANOMALOUS DIFFRACTION; EQUILIBRIUM-CONSTANTS; METHIONINE OXIDATIONmethoxinine; peptides; proteins; redox potentials; selenocysteine and tellurocysteine; selenomethionine and telluromethionine; beta-selenienylalanine and beta-tellurienylalanine; beta-thienylalanine; beta-(thienopyrrolyl)- and beta-(selenolopyrrolyl)-alanine;
 Abstract: The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium element. In the methionine series, only the sulfur-containing methionine is a proteinogenic amino acid, while selenomethionine and telluromethionine are natural amino acids that are incorporated into proteins most probably because of the tolerance of the methionyl-tRNA synthetase; so far, methoxinine the oxygen analogue has not been discovered in natural compounds. Similarly, the chalcogen analogues of tryptophan and phenylalanine in which the benzene ring has been replaced by the largely isosteric thiophene, selenophene, and more recently, even tellurophene are fully synthetic mimics that are incorporated with more or less efficiency into proteins via the related tryptophanyl- and phenylalanyl-tRNA synthetases, respectively. In the serine/cysteine series, also selenocysteine is a proteinogenic amino acid that is inserted into proteins by a special translation mechanism, while the tellurocysteine is again most probably incorporated into proteins by the tolerance of the cysteinyl-tRNA synthetase. For research purposes, all of these natural and synthetic chalcogen amino acids have been extensively applied in peptide and protein research to exploit their different physicochemical properties for modulating structural and functional properties in synthetic peptides and rDNA expressed proteins as discussed in the following review.

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Language(s): eng - English
 Dates: 20192020-02
 Publication Status: Published in print
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000503769200001
DOI: 10.1002/psc.3232
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Title: JOURNAL OF PEPTIDE SCIENCE
Source Genre: Journal
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Publ. Info: 111 RIVER ST, HOBOKEN 07030-5774, NJ USA : WILEY
Pages: - Volume / Issue: 26 (2) Sequence Number: e3232 Start / End Page: - Identifier: ISSN: 1075-2617