Green-fluorescent protein mutants with altered fluorescence excitation spectra

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

Research output: Contribution to journalArticlepeer-review

138 Scopus citations


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
Issue number2
StatePublished - Jun 26 1995


  • Fluorescence spectrometry
  • Luminescent protein
  • Mutagenesis (MeSH)

ASJC Scopus subject areas

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


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