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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
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...
Protein Folding01:22

Protein Folding

Overview
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...
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...

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Related Experiment Video

Updated: Jun 8, 2026

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
09:18

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

Protein folding disorders: toward a basic biological paradigm.

Rodrick Wallace1

  • 1Division of Epidemiology, The New York State Psychiatric Institute, Box 47, 1051 Riverside Dr., New York, NY, 10032, United States. wallace@pi.cpmc.columbia.edu

Journal of Theoretical Biology
|September 23, 2010
PubMed
Summary
This summary is machine-generated.

Current protein folding models are insufficient for understanding disease. This study introduces a new topological approach to model protein folding, offering insights into disease mechanisms and potential interventions.

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Interview: Protein Folding and Studies of Neurodegenerative Diseases
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4D Imaging of Protein Aggregation in Live Cells

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Related Experiment Videos

Last Updated: Jun 8, 2026

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
09:18

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

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

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Area of Science:

  • Biophysics
  • Computational Biology
  • Systems Biology

Background:

  • Mechanistic physics models inadequately explain protein folding and aggregation disorders.
  • In vivo paradigms are necessary for understanding disease etiology, prevention, and treatment.

Purpose of the Study:

  • To apply topological rate distortion analysis to protein folding.
  • To develop a new framework for understanding protein folding disorders.

Main Methods:

  • Topological rate distortion analysis.
  • Nonequilibrium empirical Onsager treatment.
  • Dynamic regression equations.

Main Results:

  • Identified large-scale, quasi-equilibrium 'resilience' states for normal and pathological protein folding.
  • Developed diffusion models for protein folding disorders.

Conclusions:

  • A topological approach provides a more appropriate in vivo paradigm for studying protein folding diseases.
  • Epigenetic and life history factors influence the onset rate of protein dysfunction.