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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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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 Proteins-ATCase01:19

Allosteric Proteins-ATCase

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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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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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Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Updated: Jun 13, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

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Amyloid-Driven Allostery.

Jaskiran Garcha1, Jinfeng Huang1, Karla Martinez Pomier1

  • 1Department of Chemistry and Chemical Biology, McMaster University, Hamilton, Ontario L8S 4L8, Canada.

Biophysical Chemistry
|September 15, 2024
PubMed
Summary
This summary is machine-generated.

Amyloids can control protein allostery, influencing diseases like Parkinson's. Understanding this amyloid-driven allostery reveals mutation mechanisms and suggests new therapeutic targets for proteinopathies.

Keywords:
Allostery intrinsic disordered proteinsAmyloidsCyclic adenosine monophosphate analogsGlobular signaling proteinscAMPcGMP

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Allostery and amyloid pathologies are studied separately.
  • Amyloids' role in controlling allostery is not well understood.
  • Amyloids influence allosteric effects in intrinsically disordered proteins (e.g., alpha-synuclein) and signaling proteins (e.g., protein kinase A).

Purpose of the Study:

  • To explore how amyloids control allosteric effects.
  • To explain mechanisms of disease-related mutations via amyloid-driven allostery.
  • To identify potential modulators for therapeutic interventions.

Main Methods:

  • Literature review of allostery and amyloid-related pathologies.
  • Analysis of disease-related mutations in alpha-synuclein and protein kinase A.
  • Discussion of allosteric modulators.

Main Results:

  • Amyloids drive allosteric effects in alpha-synuclein and protein kinase A.
  • Disease mutations expose amyloidogenic regions, leading to toxic or aberrant signaling amyloids.
  • Modulators like MgATP and substrates offer therapeutic potential.

Conclusions:

  • Amyloid-driven allosteric models explain disease-related mutation mechanisms.
  • Understanding these mechanisms can guide development of interventions for Parkinson's disease and cancer-related pathologies.