PMID: 9165073Mar 1, 1997Paper

Chalcogen-analogs of amino acids. Their use in X-ray crystallographic and folding studies of peptides and proteins

Biological Chemistry
D BesseLuis Moroder

Abstract

Using methionine-auxotrophic Escherichia coli strains quantitative biosynthetic replacement of the methionine residues by seleno- and telluromethionine but not by methoxinine was achieved in various model proteins, clearly indicating a limited tolerance in the editing range of methionyl-tRNA synthetase. For expression of the protein variants the acetyl derivatives of the chalcogen-analogs of methionine, obtained by a new and highly efficient synthetic procedure, proved to be the ideal source in the growth media as they were found to be significantly more stable than the underivatized methionine analogs. The conformational properties in solution, the folding and unfolding parameters as well as X-ray crystallographic data confirmed the highly isomorphous character of the atomic mutants and thus the usefulness of this concept in X-ray analysis of proteins. Quantitative replacement of cysteine residues by selenocysteine has recently been achieved using cysteine-auxotrophic E. coli strains, but a selective replacement of cysteine residues by employing the natural translational machinery of selenocysteine is also conceivable. We have therefore performed a detailed study on synthetic selenocysteine-peptides in order to determine the r...Continue Reading

References

May 12, 1992·Biochemistry·M H Chau, J W Nelson

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Citations

Dec 20, 2019·Journal of Peptide Science : an Official Publication of the European Peptide Society·Luis Moroder, Hans-Jürgen Musiol
Dec 8, 2011·Current Protocols in Nucleic Acid Chemistry·Sibo JiangZhen Huang

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