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Related Concept Videos

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...
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...
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...
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...
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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Updated: Jun 23, 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

Asymmetric kinetics of protein structural changes.

Stéphane Marchal1, Josep Font, Marc Ribó

  • 1INSERM, U710, F-34095 Montpellier, France.

Accounts of Chemical Research
|April 22, 2009
PubMed
Summary

Bidirectional pressure and temperature jump methods reveal that protein structural changes are path-dependent, challenging simple two-state transition models. This asymmetry suggests proteins adapt to stress by forming diverse conformational substates.

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Area of Science:

  • Biophysics
  • Protein Dynamics
  • Biochemistry

Background:

  • Understanding protein structural transformations is crucial for medicine and biotechnology, often requiring mechanism-based modulators.
  • Protein conformational changes are increasingly viewed through the lens of complex, high-dimensional energy landscapes.
  • Traditional methods like temperature-jump primarily observe unidirectional processes, potentially oversimplifying protein reactions.

Purpose of the Study:

  • To investigate the path-dependence of protein folding/unfolding and conformational changes.
  • To demonstrate the utility of bidirectional pressure- and temperature-jump methods for studying complex protein dynamics.
  • To challenge the prevailing assumption of simple two-state transitions in protein reactions.

Main Methods:

  • Development and application of bidirectional pressure- and temperature-jump techniques.
  • Study of ribonuclease A folding/unfolding kinetics.
  • Analysis of the allosteric transition in tryptophan synthase.

Main Results:

  • Kinetic transition states were found to be path-dependent, with rates and activation parameters varying based on perturbation direction.
  • Observed asymmetry in protein responses to pressure and temperature changes.
  • Identified the significant roles of hydration and packing defects in kinetic transition states.

Conclusions:

  • Protein reactions, including folding and allosteric transitions, exhibit path-dependent kinetics, indicating complex energy landscapes.
  • Proteins adapt to external stress by forming distinct conformational substates with unique activation barriers.
  • Bidirectional jump methods offer deeper insights into the mechanisms of physiologically relevant protein structural changes.