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This paper demonstrates that the stereoselectivity of the eukaryotic ribosome depends on the size and nature of the pendant sidechain. Interestingly, some unnatural enantiomers (e.g. [D] O-methyltyrosine) are found to be more efficiently incorporated than natural [L] residues. Incorporation of β-amino acids is also demonstrated
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Starck S.R., Olsen B., Roberts R.W. The puromycin route to assess stereo- and regiochemical constraints on peptide bond formation in eukaryotic ribosomes. J Am Chem Soc. 125:2003;8090-8091 This paper demonstrates that the stereoselectivity of the eukaryotic ribosome depends on the size and nature of the pendant sidechain. Interestingly, some unnatural enantiomers (e.g. [D] O-methyltyrosine) are found to be more efficiently incorporated than natural [L] residues. Incorporation of β-amino acids is also demonstrated.
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A comprehensive review pertaining to protein engineering using unnatural amino acid insertion
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Ellman J.A., Mendel D., Schultz P.G. Site-specific incorporation of novel backbone structures into proteins. Science. 255:1992;197-200.
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This work demonstrates that the ribosome can incorporate (aminooxy) acetic acid into different sites within the DHFR protein via nonsense suppression. The monomer has a chain length similar to β-amino acids, but has the sidechain positioned similar to a typical natural residue. The hydrazino-amino acids of Killian et al. [64] show a similar overall geometry
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A demonstration that mutant ribosomes can have relaxed stereospecificity, allowing the incorporation (acceptor and donor function) of [D] amino acids into protein chains via in vitro nonsense suppression
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Dedkova L.M., Fahmi N.E., Golovine S.Y., Hecht S.M. Enhanced D-amino acid incorporation into protein by modified ribosome. J Am Chem Soc. 125:2003;6616-6617 A demonstration that mutant ribosomes can have relaxed stereospecificity, allowing the incorporation (acceptor and donor function) of [D] amino acids into protein chains via in vitro nonsense suppression.
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