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Related Concept Videos

Aggregates Classification01:29

Aggregates Classification

317
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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Shape and Texture of Coarse Aggregate01:25

Shape and Texture of Coarse Aggregate

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Aggregate shape is classified based on the relative sharpness or roundness of the edges and corners. This classification includes categories like rounded, angular, elongated, and flaky, each with specific characteristics. Rounded aggregates, fully shaped by attrition, are typical of river or seashore gravel, while angular aggregates, such as crushed rock, have well-defined edges. Aggregates that are elongated and flaky are less desirable, as they can reduce the workability and strength of...
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Types of Aggregate Grading01:15

Types of Aggregate Grading

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Aggregate grading is crucial in economically obtaining a concrete mix with adequate strength, reasonable workability, and minimal segregation. There are four types of aggregate gradation: well-graded, uniformly (or one-sized) graded, gap-graded, and open-graded.
Well-graded aggregates include a complete range of necessary size fractions that fit together to create a dense matrix with minimal voids, represented by a smooth, continuous gradation curve. This type of grading ensures good...
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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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Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

43.6K
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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Related Experiment Video

Updated: Jun 25, 2025

Generation of Aggregates of Mouse Embryonic Stem Cells that Show Symmetry Breaking, Polarization and Emergent Collective Behaviour In Vitro
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Morphological features and types of aggregated structures.

Mansoureh Mirza Agha1, Vladimir N Uversky2

  • 1Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.

Progress in Molecular Biology and Translational Science
|May 29, 2024
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Summary

Protein aggregation causes amyloidosis, including Alzheimer's and Parkinson's diseases. Advanced techniques reveal diverse amyloid fibril structures, offering insights into these misfolding diseases.

Keywords:
AggregationAmyloidCross-βPolymorphismProtein misfolding

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Protein misfolding in vivo leads to aggregation into amyloid fibrils.
  • Amyloidosis encompasses diseases like Alzheimer's and Parkinson's, characterized by protein aggregation.
  • The structural heterogeneity of amyloid fibrils presents challenges in characterization.

Purpose of the Study:

  • To provide a concise overview of protein aggregation.
  • To focus on the structural characteristics of amyloid fibrils.
  • To highlight advancements in amyloid structure determination.

Main Methods:

  • X-ray diffraction
  • Cryo-electron microscopy
  • Solid-state Nuclear Magnetic Resonance (NMR)

Main Results:

  • Amyloid fibrils exhibit a diverse range of polymorphic structures.
  • These structures predominantly conform to the cross-β amyloid pattern.
  • Advanced techniques have provided intricate structural insights.

Conclusions:

  • Understanding amyloid fibril structure is crucial for studying misfolding diseases.
  • Technological advancements have significantly improved our ability to characterize amyloids.
  • The field of protein aggregation and amyloidosis continues to evolve with new structural data.