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 Concept Videos

Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
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...
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...
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...
Reversible or Opposing Reactions01:26

Reversible or Opposing Reactions

Reversible or opposing reactions play a crucial role in understanding the dynamic nature of chemical processes. While kinetics focuses on how reactions proceed, thermodynamics emphasizes that most reactions do not reach completion. Instead, a reverse reaction starts occurring over time, and when its rate equals that of the forward reaction, a dynamic equilibrium is established.For example, consider a simple chemical process where A forms B reversibly. The rate constants for the forward and...

You might also read

Related Articles

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

Sort by
Same author

A minimal chemo-mechanical Markov model for rotary catalysis of F<sub>1</sub>-ATPase.

Nature communications·2026
Same author

Hierarchical multi-timescale structural dynamics of the disordered N-terminal of p53.

Nature communications·2026
Same author

Phospholipid-driven conformational switching of HCV NS5A links protein folding to replication membrane remodeling.

Science advances·2026
Same author

Single-molecule dynamics reveal ATP binding alone powers substrate translocation by an ABC transporter.

Nature communications·2026
Same author

Restraining Interproton Angular and Distance Dynamics with KEnRef.

The journal of physical chemistry. B·2026
Same author

Improving Conformational Ensembles of Folded Proteins in Go̅Martini.

Journal of chemical theory and computation·2026

Related Experiment Video

Updated: Jun 14, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Braess' Paradox in Enzyme Kinetics: Asymmetry from Population Balance without Direct Cooperativity.

Malte Schäffner1, Colin A Smith1, Robert Tampé2

  • 1Theoretical and Computational Biophysics Department, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.

Journal of Chemical Theory and Computation
|February 4, 2026
PubMed
Summary

The ATPase ABCE1 protein

More Related Videos

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Hyperpolarized 13C Metabolic Magnetic Resonance Spectroscopy and Imaging
11:43

Hyperpolarized 13C Metabolic Magnetic Resonance Spectroscopy and Imaging

Published on: December 30, 2016

Related Experiment Videos

Last Updated: Jun 14, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Hyperpolarized 13C Metabolic Magnetic Resonance Spectroscopy and Imaging
11:43

Hyperpolarized 13C Metabolic Magnetic Resonance Spectroscopy and Imaging

Published on: December 30, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • The ATPase ABCE1 is crucial for ribosome recycling in eukaryotes and archaea.
  • It features two nucleotide-binding domains (NBDs) with nucleotide-binding sites (NBS) that undergo conformational changes.
  • ABCE1 exhibits unexpected asymmetric hydrolysis kinetics between its two NBSs.

Purpose of the Study:

  • To investigate the origins of the asymmetric hydrolysis kinetics in ATPase ABCE1.
  • To determine if Markov models can explain this asymmetry without invoking direct allosteric interactions between NBSs.

Main Methods:

  • Development and application of Markov models to analyze ATPase ABCE1 kinetics.
  • Utilizing a Bayesian approach to quantitatively predict experimental data.
  • Comparing kinetic data from wild-type and mutant (E485Q) NBSII.

Main Results:

  • Markov models successfully predicted the experimentally observed asymmetric kinetics and ATP occupancy.
  • The asymmetry is fully explained by structure-induced coupling between the two NBSs during opening and closing.
  • The mutation E485Q in NBSII shifts populations, bypassing a kinetic trap and accelerating turnover.

Conclusions:

  • The observed kinetic asymmetry in ATPase ABCE1 is an emergent property of coupled NBS conformational dynamics.
  • Direct allosteric interactions are not required to explain the enzyme's nonintuitive kinetics.
  • The Bayesian Markov modeling approach is applicable to other enzymes with coupled chemical/conformational dynamics.