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Related Concept Videos

Aggregates Classification01:29

Aggregates Classification

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Aggregate classification is generally based on its size, petrographic characteristics, weight, and source. Size classification ranges from coarse to fine aggregates, defined by the size of the particles. Coarse aggregates are particles that do not pass through ASTM sieve No. 4, and aggregates that pass through the sieve are fine aggregates.
Petrographic classification groups aggregates based on common mineralogical characteristics. Some of the common mineral groups found in aggregates are...
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Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

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Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Bonding and Strength of Aggregate01:12

Bonding and Strength of Aggregate

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The bond between aggregate particles and the cement matrix is significantly influenced by the shape and surface texture of the aggregates. High-strength concretes benefit from a rougher texture, which leads to stronger bonding due to greater adhesion. Angular aggregates with larger surface areas also enhance this bond. The bonding quality, however, is complex to assess as no universally accepted test exists. Good bonding is indicated when a crushed concrete specimen shows some aggregate...
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Related Experiment Video

Updated: Feb 9, 2026

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
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[FUS/TLS as a polyglutamine aggregate interacting protein].

Nobuyuki Nukina1

  • 1RIKEN Brain Science Institute Lab for Structural Neuropathology.

Rinsho Shinkeigaku = Clinical Neurology
|September 17, 2011
PubMed
Summary

Researchers identified the RNA-binding protein translocated in liposarcoma (TLS) as a key component of nuclear aggregates in polyglutamine (polyQ) diseases, including Huntington

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Context:

  • Polyglutamine (polyQ) diseases are characterized by the formation of intracellular aggregates.
  • Huntington's disease is a prominent example of a polyQ disease.

Purpose:

  • To identify the protein components of nuclear polyQ aggregates.
  • To investigate the interaction between TLS and polyQ aggregates.

Summary:

  • Mass spectrometry analysis revealed translocated in liposarcoma (TLS) as a major component of nuclear polyQ aggregates in a Huntington disease model.
  • TLS directly binds to aggregated truncated N-terminal huntingtin (tNhtt) but not to monomeric forms.
  • TLS is associated with neuronal intranuclear inclusions in Huntington disease and other polyQ disease brains.

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Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans
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Impact:

  • The sequestration of TLS in polyQ aggregates may contribute to the diverse pathological changes observed in polyQ diseases and ALS6.
  • Understanding TLS's role could offer new therapeutic targets for neurodegenerative disorders.