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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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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 Regulation01:08

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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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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 27, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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A Chemical Perspective on Allostery.

Andre A S T Ribeiro1, Vanessa Ortiz1

  • 1Department of Chemical Engineering, Columbia University , New York, New York 10027, United States.

Chemical Reviews
|January 8, 2016
PubMed
Summary

Understanding protein allosteric communication is advancing, revealing how energy transfer through residue pathways influences protein function. This review synthesizes recent computational and chemical insights into allosteric mechanisms for better predictions.

Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Computational Biology

Background:

  • Allosteric communication in proteins is crucial for regulating biological processes.
  • Understanding allostery aids in predicting protein responses to mutations and drug binding.
  • Recent decades have seen significant efforts to quantify and understand allosteric mechanisms.

Purpose of the Study:

  • To review recent advances in analyzing allosteric communication mechanisms in proteins.
  • To offer a chemically consistent perspective on allosteric mechanisms.
  • To explore the concept of allosteric pathways for signal and energy transmission.

Main Methods:

  • Review of recent computational and experimental studies on allosteric proteins.

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  • Analysis of signal propagation and conformational changes.
  • Comparison of different allosteric models and discussion of allosteric pathways.

    • Main Results:

    • Allosteric communication can be rationalized by pathways of residues transmitting energy.
    • Energy flow through these pathways can manifest as changes in protein structure and dynamics.
    • This perspective helps account for observed data in allosteric regulation.

    Conclusions:

    • Allosteric pathways provide a simplified yet powerful framework for understanding protein allostery.
    • This view integrates chemical principles with observed structural and dynamic changes.
    • Further research can build upon this simplified model to refine our understanding of complex allosteric phenomena.