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

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.4K
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...
8.4K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.9K
2.9K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.6K
2.6K
Coupled Reactions01:17

Coupled Reactions

10.0K
Cellular processes such as building and breaking down complex molecules occur through stepwise chemical reactions. Some of these chemical reactions are spontaneous and release energy, whereas others require energy to proceed. Cells often couple the energy-releasing reaction with the energy-requiring one to carry out important cell functions. 
Energy in adenosine triphosphate or ATP molecules is easily accessible to do work. ATP powers the majority of energy-requiring cellular reactions....
10.0K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

10.1K
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
10.1K
Dynamic Equilibrium02:20

Dynamic Equilibrium

60.0K
A reversible chemical reaction represents a chemical process that proceeds in both forward (left to right) and reverse (right to left) directions. When the rates of the forward and reverse reactions are equal, the concentrations of the reactant and product species remain constant over time and the system is at equilibrium. A special double arrow is used to emphasize the reversible nature of the reaction. The relative concentrations of reactants and products in equilibrium systems vary greatly;...
60.0K

You might also read

Related Articles

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

Sort by
Same author

Patterns of Dynamics Comprise a Conserved Evolutionary Trait.

Journal of molecular biology·2019
Same author

Altered dynamics may drift pathological fibrillization in membraneless organelles.

Biochimica et biophysica acta. Proteins and proteomics·2019
Same author

Optimization of reorganization energy drives evolution of the designed Kemp eliminase KE07.

Biochimica et biophysica acta·2013
Same author

Type II restriction endonucleases: structure and mechanism.

Cellular and molecular life sciences : CMLS·2005
Same author

The role of hydrophobic microenvironments in modulating pKa shifts in proteins.

Proteins·2002
Same author

Role of stabilization centers in 4 helix bundle proteins.

Proteins·2002

Related Experiment Video

Updated: Dec 2, 2025

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

9.3K

Asymmetric dynamic coupling promotes alternative evolutionary pathways in an enzyme dimer.

V Ambrus1, Gy Hoffka1, M Fuxreiter2,3

  • 1MTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.

Scientific Reports
|November 3, 2020
PubMed
Summary
This summary is machine-generated.

Enzyme evolution utilizes dynamic factors and conformational changes. A dimeric enzyme

More Related Videos

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

9.1K
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

15.8K

Related Experiment Videos

Last Updated: Dec 2, 2025

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

9.3K
Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

9.1K
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

15.8K

Area of Science:

  • Biochemistry and Molecular Biology
  • Enzymology
  • Protein Dynamics

Background:

  • Dynamic factors are increasingly recognized for their role in enzyme evolution.
  • Understanding how enzymes evolve new functions is crucial in biochemistry.

Purpose of the Study:

  • To investigate how conformational tinkering drives the evolution of new enzymatic activity.
  • To analyze the structural divergence accompanying the conversion of a dimeric phosphotriesterase to an arylesterase.

Main Methods:

  • Comparative structural analysis of enzyme subunits.
  • Investigation of loop conformation deviations and their correlation with enzyme promiscuity and specialization.
  • Analysis of dynamic coupling between subunit loops and the dimer interface.
  • Examination of co-evolutionary patterns of loop and interface residues.

Main Results:

  • Structural divergence between subunits increases with enzyme promiscuity and decreases during specialization.
  • Opposite loop movements in the two subunits are linked to dynamic coupling with the dimer interface.
  • Co-evolution of loop and interface residues supports the role of dynamic coupling.

Conclusions:

  • Protein dynamics promote conformational heterogeneity in dimeric enzymes.
  • This heterogeneity provides alternative evolutionary pathways for acquiring new functions.
  • Conformational tinkering is a key mechanism in enzyme evolution.