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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

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Related Experiment Video

Updated: May 13, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

A footnote on allostery.

F H C Crick1, Jeffries Wyman

  • 1Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, England.

Journal of Molecular Biology
|March 26, 2013
PubMed
Summary
This summary is machine-generated.

This 1965 manuscript on allosteric regulation introduces the concept of the allosteric range and provides a method for calculating the Hill coefficient. It offers a foundational interpretation of allosteric oligomers through their equivalent monomers.

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Last Updated: May 13, 2026

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • A seminal 1965 manuscript on allosteric regulation by Crick and Wyman was shared with Jacques Monod.
  • Monod shared the manuscript with Jean-Pierre Changeux, who provided a copy to Stuart Edelstein.

Observation:

  • The manuscript was never formally published but was retained and edited by Edelstein for a special issue on allostery.
  • The text focuses on interpreting allosteric oligomer properties via their equivalent monomer.

Findings:

  • The manuscript developed the concept of the allosteric range.
  • It presented a simple equation for calculating the Hill coefficient from the Monod-Wyman-Changeux model parameters.

Implications:

  • This work provides a foundational framework for understanding allosteric regulation.
  • The presented concepts and equations remain relevant for analyzing enzyme kinetics and molecular interactions.