Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Photoluminescence: Applications

Photoluminescence: Applications

Photoluminescence offers a wide range of applications due to its inherent sensitivity and selectivity. This technique allows for both direct and indirect analyses of the analyte. Direct quantitative analysis is possible when the analyte exhibits a favorable quantum yield for fluorescence or phosphorescence. However, an indirect analysis may be feasible if the analyte is not fluorescent or phosphorescent, or if the quantum yield is unfavorable. Indirect methods include reacting the analyte with...

Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Impact of the spatial distribution of positive charges on the catalytic activity of NiSOD bioinspired complexes.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2026

Same author

Minimum clinically important difference for the Urinary Symptom Profile questionnaire in people attending pulmonary rehabilitation.

Pulmonology·2026

Same author

Urinary incontinence is common among people attending pulmonary rehabilitation, yet pulmonary rehabilitation has a small effect on urinary symptoms: A multicenter prospective cohort study.

Pulmonology·2026

Same author

Biomimetic Pseudopeptides to Decipher the Interplay between Cu and Methionine-Rich Domains in Proteins.

Chemistry (Weinheim an der Bergstrasse, Germany)·2024

Same author

Outstanding Superoxide Dismutase Catalytic Activity Of Simple Peptide-Based Nickel(II) Complexes.

Angewandte Chemie (International ed. in English)·2024

Same author

An unconventional gatekeeper mutation sensitizes inositol hexakisphosphate kinases to an allosteric inhibitor.

eLife·2023

Search research articles

Related Experiment Video

Updated: Sep 25, 2025

Voltage-clamp Fluorometry in Xenopus Oocytes Using Fluorescent Unnatural Amino Acids

Voltage-clamp Fluorometry in Xenopus Oocytes Using Fluorescent Unnatural Amino Acids

Published on: May 27, 2017

A Simple Fluorescence Affinity Assay to Decipher Uranyl-Binding to Native Proteins.

Fanny Laporte¹, Yves Chenavier¹, Alexandra Botz¹

¹IRIG, SyMMES, Université Grenoble Alpes, CEA, CNRS, Grenoble INP, 38000, Grenoble, France.

Angewandte Chemie (International Ed. in English)

|April 25, 2022

Summary

This study introduces a simple fluorescence-based method to measure how strongly proteins bind to uranyl. This new tool helps understand uranyl toxicity and develop better treatments.

Keywords:

Binding Affinity Bioinorganic Chemistry Fluorescent Probe Peptide/Proteins Uranium

More Related Videos

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Published on: October 21, 2016

Effect of Fluorescent Proteins on Fusion Partners Using Polyglutamine Toxicity Assays in Yeast

Effect of Fluorescent Proteins on Fusion Partners Using Polyglutamine Toxicity Assays in Yeast

Published on: November 28, 2018

Related Experiment Videos

Last Updated: Sep 25, 2025

Voltage-clamp Fluorometry in Xenopus Oocytes Using Fluorescent Unnatural Amino Acids

Voltage-clamp Fluorometry in Xenopus Oocytes Using Fluorescent Unnatural Amino Acids

Published on: May 27, 2017

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Published on: October 21, 2016

Effect of Fluorescent Proteins on Fusion Partners Using Polyglutamine Toxicity Assays in Yeast

Effect of Fluorescent Proteins on Fusion Partners Using Polyglutamine Toxicity Assays in Yeast

Published on: November 28, 2018

Area of Science:

Biochemistry
Analytical Chemistry
Toxicology

Background:

Uranyl toxicity necessitates understanding protein-uranyl interactions.
Existing methods for assessing uranyl-protein affinity are complex and require specialized equipment.
Developing accessible methods is crucial for toxicity studies and decorporation strategies.

Purpose of the Study:

To develop a simple, efficient, fluorescence-based assay for quantifying uranyl-protein and uranyl-peptide binding affinities.
To establish a reference scale for uranyl affinity in solution.
To validate the assay using native proteins.

Main Methods:

Design and characterization of a novel uranyl-binding fluorescent probe.
Utilizing fluorescence signal quenching to determine binding affinity.
Building a reference scale based on high-affinity uranyl-binding peptides.
Validation of the method with four native proteins.

Main Results:

A novel fluorescent probe for uranyl detection was successfully developed and characterized.
A reliable reference scale for uranyl affinity in solution was established.
The fluorescence-based method accurately re-evaluated uranyl-binding affinities of native proteins.

Conclusions:

The developed fluorescence-based method provides a simple and efficient way to assess uranyl-protein and uranyl-peptide affinities.
This tool facilitates reproducible and reliable measurements, aiding in the study of uranyl toxicity and decorporation.
The assay is adaptable for various peptides and proteins, offering broad applicability.