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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Fast Reactions01:27

Fast Reactions

Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Transition State Theory01:25

Transition State Theory

Transition-state theory, also known as activated-complex theory, provides a molecular-level explanation of reaction rates in both gas-phase and solution-phase reactions. It extends earlier kinetic models by considering the formation of a short-lived, high-energy configuration during a reaction.The progress of a chemical reaction can be represented using a reaction profile, which plots potential energy against the reaction coordinate. As two reactant molecules approach one another, their...
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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Related Experiment Video

Updated: May 29, 2026

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Time-dependent intermolecular interaction during protein reactions.

Masahide Terazima1

  • 1Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan. mterazima@kuchem.kyoto-u.ac.jp

Physical Chemistry Chemical Physics : PCCP
|September 6, 2011
PubMed
Summary

A new pulsed laser technique monitors intermolecular reaction kinetics by measuring time-dependent diffusion coefficients. This method successfully detects real-time biomolecular interactions like transient association and dissociation in solution.

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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

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Related Experiment Videos

Last Updated: May 29, 2026

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Area of Science:

  • Physical Chemistry
  • Biophysics
  • Chemical Kinetics

Background:

  • Monitoring reaction kinetics of intermolecular interactions is crucial for understanding complex biological and chemical processes.
  • Existing techniques may have limitations in real-time detection or sensitivity for transient events.

Purpose of the Study:

  • To present a novel method for monitoring reaction kinetics of intermolecular interactions.
  • To demonstrate the capability of this method in detecting time-dependent biomolecular interactions in real-time.

Main Methods:

  • Utilizes time-dependent diffusion coefficient measurements.
  • Employs the pulsed laser-induced transient grating (PITG) technique.
  • Analyzes transient association and dissociation reactions in solution.

Main Results:

  • Successfully detected time-dependent biomolecular interactions in real-time.
  • Demonstrated the ability to monitor reaction kinetics of intermolecular interactions.
  • Provided a detailed comparison with other existing techniques, highlighting unique features.

Conclusions:

  • The pulsed laser-induced transient grating method offers a powerful tool for real-time kinetic studies of intermolecular interactions.
  • This technique is particularly valuable for observing transient molecular events in solution.
  • The method provides unique insights compared to conventional approaches for kinetic analysis.