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Cooperative Allosteric Transitions

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 Transitions

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 Transitions

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 Regulation

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 Regulation

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...

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Related Experiment Video

Updated: May 7, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Collective dynamics underlying allosteric transitions in hemoglobin.

Martin D Vesper¹, Bert L de Groot

¹Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.

Plos Computational Biology

|September 27, 2013

Summary

This summary is machine-generated.

This study reveals hemoglobin's allosteric mechanism using novel computational methods, detailing how tertiary and quaternary motions couple to enable subunit communication and explain the Bohr effect.

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Measurement of Heme Synthesis Levels in Mammalian Cells

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Area of Science:

Biophysics
Computational Biology
Structural Biology

Background:

Hemoglobin is a key allosteric protein, but its precise molecular mechanism of cooperativity remains incompletely understood.
Understanding allosteric regulation is crucial for deciphering protein function and designing targeted therapeutics.

Purpose of the Study:

To elucidate the atomistic-level mechanism of cooperativity in hemoglobin.
To analyze the coupling between tertiary and quaternary motions during allosteric transitions.

Main Methods:

Development of a novel computational technique to analyze motion coupling.
Utilizing Molecular Dynamics simulations to capture spontaneous quaternary transitions.
Application of Functional Mode Analysis to separate and analyze tertiary-only and quaternary-only motion subspaces.

Main Results:

Identification of a collective coordinate within tertiary motions directly correlated with quaternary motions, revealing the allosteric coupling mechanism.
Demonstration that hemoglobin's inter-subunit communication relies on both hydrogen bonds and steric interactions.
Observation that histidine protonation states influence T-to-R transition rates, offering an atomistic basis for the Bohr effect.

Conclusions:

The study provides unprecedented atomistic insight into hemoglobin's allosteric mechanism and cooperativity.
The findings highlight the interplay of distinct motion types and non-covalent interactions in allosteric regulation.
This work offers a potential molecular explanation for the Bohr effect, linking protein structure to physiological function.