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Science 10 January 1992:
Vol. 255. no. 5041, pp. 197 - 200
DOI: 10.1126/science.1553546
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Articles

Science, Vol 255, Issue 5041, 197-200
Copyright © 1992 by American Association for the Advancement of Science

articles

Site-specific incorporation of novel backbone structures into proteins

JA Ellman, D Mendel, and PG Schultz

Department of Chemistry, University of California, Berkeley 94720.

A number of unnatural amino acids and amino acid analogs with modified backbone structures were substituted for alanine-82 in T4 lysozyme. Replacements included alpha,alpha-disubstituted amino acids, N-alkyl amino acids, and lactic acid, an isoelectronic analog of alanine. The effects of these electronic and structural perturbations on the stability of T4 lysozyme were determined. The relatively broad substrate specificity of the Escherichia coli protein biosynthetic machinery suggests that a wide range of backbone and side-chain substitutions can be introduced, allowing a more precise definition of the factors affecting protein stability.


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Initiating translation with D-amino acids.
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Enzymatic aminoacylation of tRNA with unnatural amino acids.
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An Expanded Eukaryotic Genetic Code.
J. W. Chin, T. A. Cropp, J. C. Anderson, M. Mukherji, Z. Zhang, and P. G. Schultz (2003)
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Synthesis of proteins by native chemical ligation.
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Neutrophil activation by monomeric interleukin-8.
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Probing the structure and mechanism of Ras protein with an expanded genetic code.
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Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected].
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An Efficient Antibody-Catalyzed Aminoacylation Reaction.
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