Abstract

Metalloproteins contain highly specialized metal-binding sites that are designed to accept specific metal ions to maintain correct function. Although many of the sites have been modified with success, the relative paucity of functional group availability within proteinogenic amino acids can sometimes leave open questions about specific functions of the metal binding ligands. Attaining a more thorough analysis of individual amino acid function within metalloproteins has been realized using expressed protein ligation (EPL). Here we describe our recent efforts using EPL to incorporate nonproteinogenic cysteine and methionine analogues into the type 1 copper site found in Pseudomonas aeruginosa azurin.

Original languageEnglish
Pages (from-to)97-115
Number of pages19
JournalMethods in Enzymology
Volume462
DOIs
StatePublished - Jul 24 2009

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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