Infrared Fluorescent Protein iRFP as an Acceptor for Förster Resonance Energy Transfer

O. A. Zlobovskaya, K. S. Sarkisyan, K. A. Lukyanov

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

Bacteriophytochrome-based infrared fluorescent protein iRFP was tested as an acceptor for F6rster resonance energy transfer (FRET). Far-red GFP-like fluorescent proteins mKate2, eqFP650, and eqFP670 were used as donors; Bacterial expression vectors encoding donor and acceptor proteins fused by a 17-amino acid linker were.constructed. FRET for purified proteins in vitro was, estimated from increase of the donor emission after digestion of the linker. Among the three constructs tested, the most efficient FRET (approximately 30%) was detected for the eqFP650-iRFP pair.

Original languageEnglish
Pages (from-to)299-304
Number of pages6
JournalBioorganicheskaia khimiia
Volume41
Issue number3
DOIs
Publication statusPublished - 1 May 2015
Externally publishedYes

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