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Related Concept Videos

Protein Dynamics in Living Cells01:19

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...

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Related Experiment Video

Updated: Jul 5, 2026

Structural Information from Single-molecule FRET Experiments Using the Fast Nano-positioning System
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Published on: February 9, 2017

Two-step FRET as a structural tool.

Heather M Watrob1, Chia-Pin Pan, Mary D Barkley

  • 1Department of Chemistry, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, Ohio 44106-7078, USA.

Journal of the American Chemical Society
|June 12, 2003
PubMed
Summary

This study introduces a new theoretical framework for using Förster Resonance Energy Transfer (FRET) with multiple chromophores to measure distances in molecular complexes. The approach expands FRET

Area of Science:

  • Biophysics
  • Molecular Biology
  • Spectroscopy

Background:

  • Förster Resonance Energy Transfer (FRET) is a powerful technique for studying molecular interactions and distances.
  • Traditional FRET typically involves one donor and one acceptor chromophore.
  • Studying complex molecular systems often requires more sophisticated FRET approaches.

Purpose of the Study:

  • To present a general theoretical framework for distance measurements in three-chromophore systems using FRET.
  • To explore and derive equations for efficiencies in multiple energy transfer schemes.
  • To discuss labeling strategies for diagnosing energy transfer pathways and enabling distance measurements.

Main Methods:

  • Development of a theoretical framework for three-chromophore FRET systems.

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Last Updated: Jul 5, 2026

Structural Information from Single-molecule FRET Experiments Using the Fast Nano-positioning System
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High Precision FRET at Single-molecule Level for Biomolecule Structure Determination
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High Precision FRET at Single-molecule Level for Biomolecule Structure Determination

Published on: May 13, 2017

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07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

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  • Derivation of equations for energy transfer efficiencies in donor quenching and sensitized emission measurements.
  • Experimental validation using model systems with known structures and steady-state/lifetime quenching techniques.

    • Main Results:

    • The study considers three distinct energy transfer schemes: two-step relay, single donor to multiple acceptors, and a combined two-step relay.
    • Theoretical predictions are supported by experimental data from model systems.
    • Measured distances in three-chromophore systems align with those from two-chromophore systems and molecular models.

    Conclusions:

    • The presented theoretical framework successfully expands the application of FRET for studying complex molecular assemblies.
    • The methodology allows for accurate distance measurements in systems with multiple FRET interactions.
    • The findings provide a foundation for advanced FRET applications in molecular science.