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Related Concept Videos

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 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...
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 17, 2026

Imaging G-protein Coupled Receptor (GPCR)-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum
09:40

Imaging G-protein Coupled Receptor (GPCR)-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum

Published on: September 20, 2011

Perfect adaptation in eukaryotic gradient sensing using cooperative allosteric binding.

Vishnu Srinivasan1, Wei Wang1, Brian A Camley1,2

  • 1Johns Hopkins University, Department of Physics and Astronomy, Baltimore, Maryland 21218, USA.

Physical Review. E
|May 16, 2026
PubMed
Summary
This summary is machine-generated.

Eukaryotic cells adapt to chemical gradients using an internal protein that modulates receptor sensitivity. This mechanism allows for precise chemotaxis across various concentrations, balancing adaptation speed with accuracy.

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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Imaging G-protein Coupled Receptor (GPCR)-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum
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Published on: September 20, 2011

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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

Area of Science:

  • Cellular Biology
  • Biophysics
  • Biochemistry

Background:

  • Eukaryotic cells sense chemical gradients via membrane receptors for chemotaxis.
  • Adaptation to varying ligand concentrations is crucial for effective chemotaxis.

Purpose of the Study:

  • To present a model for eukaryotic gradient sensing and chemotaxis adaptation.
  • To investigate how an internal allosteric factor influences receptor-ligand binding affinity and cellular sensitivity.

Main Methods:

  • Developed a mathematical model for gradient sensing incorporating an allosteric factor.
  • Proposed a reaction scheme for regulating the allosteric factor's availability.
  • Calculated bounds on chemotactic accuracy and analyzed the impact of diffusion rates.

Main Results:

  • An interior protein (allosteric factor) can increase receptor-ligand binding affinity, enabling adaptation to different concentrations.
  • The cell can achieve near-optimal chemotaxis over a wide range of ligand concentrations.
  • Chemotactic accuracy is sensitive to the diffusion rate of the allosteric compound relative to reaction rates.

Conclusions:

  • The proposed allosteric mechanism allows eukaryotic cells to adapt their sensitivity for robust chemotaxis.
  • A trade-off exists between adaptation time and gradient sensing accuracy, influenced by molecular diffusion.
  • This model provides insights into the biophysical basis of cellular chemotaxis.