Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Nonequilibrium dynamic mechanism for allosteric effect.

Jianhua Xing1

  • 1Chemistry, Materials and Life Sciences Directorate, University of California, Livermore, California 94550, USA. jxing@vt.edu

Physical Review Letters
|November 13, 2007
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Hook stiffness as a mechanical switch for torque regulation in the bacterial flagellar motor.

Biophysical journal·2026
Same author

Single cell snapshot analyses under proper representation reveal that epithelial-mesenchymal transition couples at G1 and G2/M.

Communications biology·2026
Same author

Pulmonary Microvascular Endothelial Antigen Presentation Activates resident CD8<sup>+</sup> T Cells to Restrain Influenza Lung Injury.

Research square·2026
Same author

A Roadmap for the Future of Systems Biology in Cancer Research.

Cancer research·2025
Same author

GraphVelo allows for accurate inference of multimodal velocities and molecular mechanisms for single cells.

Nature communications·2025
Same author

Transiently increased coordination in gene regulation during cell phenotypic transitions.

PRX life·2025
Same journal

Erratum: Bacterial Turbulence at Compressible Fluid Interfaces [Phys. Rev. Lett. 136, 138301 (2026)].

Physical review letters·2026
Same journal

Unveiling Light-Quark Yukawa Flavor Structure via Dihadron Fragmentation at Lepton Colliders.

Physical review letters·2026
Same journal

Adaptable Route to Fast Coherent State Transport via Bang-Bang-Bang Protocols.

Physical review letters·2026
Same journal

Topological Transition and Emergence of Elasticity of Dislocation in Skyrmion Lattice: Beyond Kittel's Magnetic-Polar Analogy.

Physical review letters·2026
Same journal

Pound-Drever-Hall Method for Superconducting-Qubit Readout.

Physical review letters·2026
Same journal

Coupling a ^{73}Ge Nuclear Spin to an Electrostatically Defined Quantum Dot in Silicon.

Physical review letters·2026
See all related articles

Regulating molecules may alter enzyme function by changing protein dynamics, not just thermodynamics. This new mechanism affects temperature dependence and enzyme activity patterns, with experimental tests proposed.

Area of Science:

  • Biochemistry
  • Chemical Physics
  • Enzyme Kinetics

Background:

  • Allosteric regulation is traditionally understood through thermodynamic principles.
  • Enzymatic reactions involve complex protein internal motions and potential energy barriers.
  • Existing models may not fully capture the dynamic nature of enzyme regulation.

Purpose of the Study:

  • To propose a new mechanism for allosteric regulation based on nonequilibrium protein dynamics.
  • To investigate how regulating molecules influence enzyme internal motions.
  • To predict distinct experimental signatures of this dynamic regulatory mechanism.

Main Methods:

  • Theoretical modeling of enzyme reaction cycles incorporating protein internal motions.
  • Analysis of how effector molecules perturb nonequilibrium protein dynamics.

Related Experiment Videos

  • Derivation of predictions for temperature dependence and waiting time distributions.
  • Main Results:

    • The proposed theory predicts altered temperature dependence for enzymes regulated by nonequilibrium dynamics.
    • Enzyme turnover cycle waiting time distributions are predicted to differ with and without effectors.
    • Dynamic fluctuation patterns of enzymes are expected to change in the presence of regulatory molecules.

    Conclusions:

    • Allosteric regulation may involve modulation of nonequilibrium protein dynamics, extending beyond thermodynamic control.
    • The proposed mechanism offers a new framework for understanding enzyme regulation.
    • Distinct, experimentally testable predictions are provided for validating the theory.