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Related Concept Videos

Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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 a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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 a mild...
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...
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...

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Related Experiment Video

Updated: Jun 7, 2026

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

Dynamic model for enzyme action.

Qinyi Zhao1

  • 1Department of Biochemistry and Molecular Biology, Medical Institute, P. O. Box 2619, Beijing 100068, PR China.

Protein and Peptide Letters
|November 9, 2010
PubMed
Summary

Protein thermodynamic structure theory links enzyme reaction timescales to protein dynamics and conformational changes. This approach provides a framework for understanding enzyme catalysis and activity.

Area of Science:

  • Biophysics
  • Biochemistry
  • Enzymology

Background:

  • Protein thermodynamic structure theory integrates protein dynamics and enzyme catalysis mechanisms.
  • The timescale of enzymatic reactions (TER) is crucial for characterizing enzyme conformational changes.
  • Key aspects of TER include its relation to protein main chain motions and its role in defining conformational change scope.

Purpose of the Study:

  • To examine a hypothesis derived from protein thermodynamic structure theory.
  • To investigate the relationship between the timescale of enzymatic reactions and protein dynamics.
  • To explore how protein main chain motions influence enzyme activity.

Main Methods:

  • Analysis based on protein thermodynamic structure theory.
  • Examination of the timescale of enzymatic reactions (TER).

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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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Last Updated: Jun 7, 2026

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

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Modeling an Enzyme Active Site using Molecular Visualization Freeware
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  • Linking TER to internal protein main chain motions and conformational change scope.

    • Main Results:

    • The timescale of enzymatic reactions (TER) is logically related to internal protein main chain motions.
    • TER sets the upper limit for the scope of protein conformational changes.
    • Feature (i) of TER connects to enzyme-reactant complex dynamics; Feature (ii) links to dynamic sites involved in enzyme activity.

    Conclusions:

    • A comprehensive understanding of enzymology can be achieved using protein thermodynamic structure theory.
    • The study establishes the significance of TER in understanding enzyme mechanisms.
    • Protein dynamics and conformational changes are central to enzyme catalysis.