Unnatural amino acid mutagenesis of fluorescent proteins

Feng Wang, Wei Niu, Jiantao Guo, Peter G. Schultz

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Tyrosine 66 of a green fluorescent protein (GFP) was substituted with unnatural amino acids carrying boronate, azido, nitro, and keto substituents. In general, the λem values of these GFP mutants is blue-shifted relative to that of GFP, and the fluorescence intensity of the boronate variant increases upon oxidation (see scheme). The X-ray crystal structures of the keto and boronate GFP mutants provide explanations of their altered fluorescence properties.

Original languageEnglish (US)
Pages (from-to)10132-10135
Number of pages4
JournalAngewandte Chemie - International Edition
Volume51
Issue number40
DOIs
StatePublished - Oct 1 2012

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Mutagenesis
Green Fluorescent Proteins
Amino acids
Proteins
Amino Acids
Fluorescence
Tyrosine
Crystal structure
X rays
Oxidation

Keywords

  • biosensors
  • fluorescence
  • fluorescent proteins
  • protein engineering
  • unnatural amino acids

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

Cite this

Unnatural amino acid mutagenesis of fluorescent proteins. / Wang, Feng; Niu, Wei; Guo, Jiantao; Schultz, Peter G.

In: Angewandte Chemie - International Edition, Vol. 51, No. 40, 01.10.2012, p. 10132-10135.

Research output: Contribution to journalArticle

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