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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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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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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...
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Allosteric Proteins-ATCase01:19

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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...
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Updated: Mar 18, 2026

Extracellular Multi-Unit Recording from the Olfactory Nerve of Teleosts
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Allosteric proteins as logarithmic sensors.

Noah Olsman1, Lea Goentoro2

  • 1Department of Computing and Mathematical Sciences, California Institute of Technology, Pasadena, CA 91125;

Proceedings of the National Academy of Sciences of the United States of America
|July 14, 2016
PubMed
Summary

Logarithmic sensing, crucial for biological systems, can be achieved using single allosteric proteins. This mechanism allows systems to respond to signal changes proportionally, regardless of the initial signal level.

Keywords:
allosteric regulationfold-change detectionlogarithmic sensing

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Systems Biology

Background:

  • Many biological systems, including vision and cellular signaling, detect fold changes in stimuli relative to background noise.
  • This fold-change detection necessitates sensing signals on a logarithmic scale, responding equally to proportional changes.
  • Implementing molecular-level logarithmic sensors remains an active area of research.

Purpose of the Study:

  • To investigate the potential of allosteric regulation in implementing molecular-level logarithmic sensing.
  • To demonstrate that single allosteric proteins can function as logarithmic sensors.

Main Methods:

  • Utilized mathematical modeling to analyze the response of allosteric proteins to stimuli.
  • Reviewed existing literature data on allosteric protein behavior and parameter regimes.
  • Identified biological systems where fold-change detection is critical and examined the role of allosteric proteins within them.

Main Results:

  • Mathematical models indicate that allosteric proteins can exhibit logarithmic sensing capabilities.
  • Literature data suggests that certain allosteric proteins operate within parameter ranges conducive to logarithmic sensing.
  • Allosteric proteins are prevalent in biological systems known for fold-change detection.

Conclusions:

  • Allosteric regulation provides a viable mechanism for achieving logarithmic sensing at the molecular level.
  • Allosteric proteins are likely utilized as logarithmic sensors in various biological processes.
  • This finding broadens the understanding of allosteric protein function in biological signal processing.