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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Protein Folding01:25

Protein Folding

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
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

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Nucleic acid-mediated protein aggregation and assembly.

Changlin Liu1, Yong Zhang

  • 1Key Laboratory of Pesticide and Chemical Biology, Ministry of Education, and School of Chemistry, Central China Normal University, Wuhan, China.

Advances in Protein Chemistry and Structural Biology
|August 18, 2011
PubMed
Summary

Nucleic acids significantly accelerate amyloid protein aggregation by binding electrostatically and acting as a template. This interaction alters protein conformation and promotes the formation of insoluble deposits characteristic of various diseases.

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Last Updated: May 30, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
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Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Amyloid proteins aggregate into β-sheet-rich fibrils in various tissues.
  • These aggregates are associated with polyanionic species like nucleic acids and polysaccharides.
  • Nucleic acids are found in amyloid deposits in diseases such as Alzheimer's disease.

Purpose of the Study:

  • To investigate the role of nucleic acids in amyloid protein aggregation.
  • To understand the binding affinity and interactions between amyloid proteins and nucleic acids.
  • To elucidate the mechanism by which nucleic acids influence amyloid formation.

Main Methods:

  • Analysis of amyloid protein and nucleic acid interactions.
  • Examination of conformational changes in amyloid proteins upon nucleic acid binding.
  • Investigating the templating effect of nucleic acids on amyloid aggregation.

Main Results:

  • Amyloid proteins exhibit high binding affinity for nucleic acids, primarily through electrostatic interactions.
  • Nucleic acids induce and accelerate amyloid protein aggregation.
  • A template effect, restricting protein orientation and increasing local concentration, enhances aggregation.

Conclusions:

  • Nucleic acids play a crucial role in promoting and accelerating amyloid protein aggregation.
  • The interaction involves electrostatic binding and a template mechanism.
  • Nucleic acids can be integral components of amyloid aggregates.