Metal ion accessibility of histidine-modified superfolder green fluorescent protein expressed in Escherichia coli

Research output: Contribution to journalArticle

Abstract

Green fluorescent protein (GFP) is frequently utilized for metal ion detection and quantification. To improve the metal binding potential of GFP, three residues (N146, F165, and L201) were substituted to histidines. Each variant responded differently upon interaction with metal ions. More than 80% of N146H, having the most accessible surface area, could bind to immobilized metal ions. However, only F165H exhibited significant differences in quenching by soluble metal ions (22% fluorescence decrease) in comparison with the template protein (12%). These findings can be utilized for designing GFP variants for metal binding and sensor applications.

Details

Authors
  • Natta Tansila
  • Kristian Becker
  • Chartchalerm Isarankura Na-Ayudhya
  • Virapong Prachayasittikul
  • Leif Bülow
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biochemistry and Molecular Biology

Keywords

  • metal binding, histidine, protein, green fluorescent, accessible surface area, fluorescent quenching
Original languageEnglish
Pages (from-to)1391-1396
JournalBiotechnology Letters
Volume30
Issue number8
Publication statusPublished - 2008
Publication categoryResearch
Peer-reviewedYes