An intrinsic FRET sensor of protein–ligand interactions-Reference-Cited by-同舟云学术

An intrinsic FRET sensor of protein–ligand interactions

Published:2020 Issue:21 Volume:18 Page:4079-4084
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Gleason Patrick R.¹²³⁴^ORCID,Kelly Patrick I.¹²³⁴^ORCID,Grisingher Dominic W.¹²³⁴^ORCID,Mills Jeremy H.¹²³⁴^ORCID

Affiliation:

1. School of Molecular Sciences and The Biodesign Center for Molecular Design and Biomimetics

2. Arizona State University

3. Tempe

4. USA

Abstract

The non-canonical amino acid l-(7-hydroxycoumarin-4-yl)ethylglycine can serve as a FRET acceptor from tryptophan. Here, we demonstrate how this amino acid pair can be used to generate an intrinsic FRET-based sensor of protein–ligand interactions.

Funder

National Institute of General Medical Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/OB/D0OB00793E

Reference25 articles.

1. Probing Protein Folding Using Site-Specifically Encoded Unnatural Amino Acids as FRET Donors with Tryptophan

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4. Site-Specific Fluorescent Labeling of Nascent Proteins on the Translating Ribosome

5. Efficient Synthesis and In Vivo Incorporation of Acridon-2-ylalanine, a Fluorescent Amino Acid for Lifetime and Förster Resonance Energy Transfer/Luminescence Resonance Energy Transfer Studies

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