Green-fluorescent protein mutants with altered fluorescence excitation spectra

Torsten Ehrig, Dennis J. O'Kane, Franklyn G. Prendergast

Research output: Contribution to journalArticle

137 Citations (Scopus)

Abstract

Using random mutagenesis and visual selection of fluorescent clones, we have isolated a T2031 and a E222G mutant of the Aequorea green-fluorescent protein. Each mutant has one of the two fluorescence excitation bands of the wild type deleted and retains the other without a wavelength shift. This finding is consistent with each excitation band corresponding to a distinct spectroscopic state of the chromophore. Both mutations are single amino acid exchanges which in the linear sequence are located remotely from the chromophore but in the folded protein may be situated in its vicinity. We conclude that the mutations influence the fluorescence properties by changing the interactions between the chromophore and its protein environment.

Original languageEnglish (US)
Pages (from-to)163-166
Number of pages4
JournalFEBS Letters
Volume367
Issue number2
DOIs
StatePublished - Jun 26 1995

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Chromophores
Green Fluorescent Proteins
Fluorescence
Mutation
Mutagenesis
Proteins
Clone Cells
Amino Acids
Wavelength

Keywords

  • Fluorescence spectrometry
  • Luminescent protein
  • Mutagenesis (MeSH)

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

Green-fluorescent protein mutants with altered fluorescence excitation spectra. / Ehrig, Torsten; O'Kane, Dennis J.; Prendergast, Franklyn G.

In: FEBS Letters, Vol. 367, No. 2, 26.06.1995, p. 163-166.

Research output: Contribution to journalArticle

Ehrig, Torsten ; O'Kane, Dennis J. ; Prendergast, Franklyn G. / Green-fluorescent protein mutants with altered fluorescence excitation spectra. In: FEBS Letters. 1995 ; Vol. 367, No. 2. pp. 163-166.
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