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Related Concept Videos

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...
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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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
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.
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Protein Folding01:22

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Related Experiment Video

Updated: Jul 15, 2026

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

How crowding shapes protein aggregation.

Tejas Nikam1, Shashi Prakash Patel2, Shubhini A Saraf1

  • 1Department of Pharmaceutics, National Institute of, Pharmaceutical Education and Research, Raebareli (NIPER-R), Lucknow, Uttar Pradesh, 226002 India.

Current Opinion in Structural Biology
|July 13, 2026
PubMed
Summary

Macromolecular crowding influences protein aggregation in neurodegenerative diseases by promoting phase separation and concentrating proteins. Targeting these early states, not just fibrils, may offer new therapeutic strategies.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Macromolecular crowding affects protein structures, particularly those linked to neurodegeneration.
  • Crowding can induce liquid-liquid phase separation (LLPS), forming protein condensates.

Purpose of the Study:

  • To explore the role of macromolecular crowding in protein aggregation and neurodegeneration.
  • To investigate the continuum of crowding, LLPS, and aggregation.
  • To identify new therapeutic targets for neurodegenerative diseases.

Main Methods:

  • In-cell nuclear magnetic resonance (NMR)
  • Cryo-electron microscopy (cryo-EM) of condensates
  • Single-molecule methods
  • Thermodynamic-kinetic modeling

Main Results:

  • Crowding enriches aggregation-prone states and alters nucleation.
  • Crowding promotes LLPS, concentrating proteins and promoting liquid-to-solid transitions into amyloid assemblies.
  • Dilute solution assays may not reflect in-cell mechanisms.

Conclusions:

  • The crowding-LLPS-aggregation continuum is crucial for understanding neurodegenerative disease mechanisms.
  • Crowding-aware structural biology is essential for studying cellular protein behavior.
  • Targeting condensate properties and early oligomers offers novel therapeutic avenues.