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Site-specific incorporation of novel backbone structures into proteins

Academic Article
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Overview

authors

  • Ellman, J. A.
  • Mendel, D.
  • Schultz, Peter

publication date

  • January 1992

journal

  • Science  Journal

abstract

  • 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.

subject areas

  • Alanine
  • Amino Acid Sequence
  • Amino Acids
  • Circular Dichroism
  • Codon
  • Enzyme Stability
  • Escherichia coli
  • Muramidase
  • Mutagenesis, Site-Directed
  • Protein Conformation
  • Structure-Activity Relationship
  • Substrate Specificity
  • T-Phages
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1553546

PubMed ID

  • 1553546
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Additional Document Info

start page

  • 197

end page

  • 200

volume

  • 255

issue

  • 5041

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