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Updated: Jun 10, 2026

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
Fluorescent ribonucleoside as a FRET acceptor for tryptophan in native proteins
Yun Xie1, Tucker Maxson, Yitzhak Tor
1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, USA.
None:
A new fluorescent ribonucleoside analogue, containing 5-aminoquinazoline-2,4(1H,3H)-dione, acts as a Forster resonance energy transfer acceptor for tryptophan (R(0) = 22 A) and displays visible emission (440 nm). As tryptophan is frequently found at or near the recognition domains of RNA binding proteins, this FRET pair facilitates the study of RNA binding to native proteins and peptides, which is demonstrated here for the HIV-1 Rev association with the Rev Response Element (RRE).

