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Updated: Feb 4, 2026
06:02
Determining the Thermodynamic and Kinetic Association of a DNA Aptamer and Tetracycline Using Isothermal Titration Calorimetry
Published on: August 23, 2022
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SNAREpin Assembly: Kinetic and Thermodynamic Approaches
Feng Li1, Frederic Pincet2,3
1Department of Cell Biology and Nanobiology Institute, School of Medicine, Yale University, New Haven, CT, USA. feng.li@yale.edu.
Methods in Molecular Biology (Clifton, N.J.)
|October 15, 2018
Summary
This study introduces isothermal titration calorimetry and fluorescence anisotropy to measure protein complex assembly and disassembly kinetics. These methods help identify key factors influencing protein complex formation dynamics.
Area of Science:
- Biochemistry and Molecular Biology
- Biophysics
Background:
- Protein complexes are crucial for biological processes.
- Understanding the kinetics and thermodynamics of protein complex assembly and disassembly is vital for deciphering cellular functions.
Purpose of the Study:
- To present efficient techniques for quantifying protein complex assembly and disassembly.
- To demonstrate the application of these techniques using SNAREpin formation as an example.
- To identify critical factors that modulate assembly kinetics.
Main Methods:
- Isothermal titration calorimetry (ITC)
- Fluorescence anisotropy (FA)
- SNARE protein preparation
Main Results:
- Demonstrated the utility of ITC and FA for characterizing protein complex dynamics.
- Provided a protocol for preparing SNARE proteins for biophysical assays.
- Showcased how these methods can reveal factors influencing assembly kinetics.
Conclusions:
- Isothermal titration calorimetry and fluorescence anisotropy are effective tools for studying protein complex dynamics.
- Accurate kinetic and thermodynamic characterization of protein complexes enhances understanding of biological processes.
- The presented methods facilitate the identification of key regulators of protein assembly.
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