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A new trend to determine biochemical parameters by quantitative FRET assays
Jia-yu Liao1,2,3, Yang Song1, Yan Liu1
1Department of Bioengineering, University of California at Riverside, 900 University Avenue, Riverside, CA 92521, USA.
Acta Pharmacologica Sinica
|November 17, 2015
Summary
Förster resonance energy transfer (FRET) assays can quantify molecular interactions and biochemical parameters like binding affinity and enzyme kinetics. This review explores FRET
Area of Science:
- Biophysics
- Biochemistry
- Molecular Biology
Background:
- Förster resonance energy transfer (FRET) is a biophysical technique used to measure molecular interactions within 1-10 nm.
- FRET efficiency is highly sensitive to the distance between donor and acceptor molecules.
- Traditionally, FRET has been used for quantitative distance measurements.
Purpose of the Study:
- To highlight the underutilized potential of FRET assays for quantifying molecular interactions.
- To review the application of quantitative FRET for determining biochemical parameters.
- To discuss FRET-based methods for in-cell and in-solution analyses.
Main Methods:
- Discussion of quantitative Förster resonance energy transfer (FRET) assays.
- Description of fluorescent microscopy-based FRET for in-cell studies.
- Description of fluorimeter-based FRET for solution-based studies.
Main Results:
- Quantitative FRET assays can accurately determine biochemical parameters.
- Examples include dissociation constant (K(d)), enzymatic velocity (k(cat)), and K(m).
- Both microscopy and fluorimetry enable quantitative FRET measurements.
Conclusions:
- Quantitative FRET assays offer a powerful tool for characterizing molecular interactions and enzyme kinetics.
- These methods are applicable in both cellular and solution environments.
- Further exploitation of FRET signals can advance biological and biomedical research.
