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Related Concept Videos

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
Protein Folding01:22

Protein Folding

Overview
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...
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...
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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Related Experiment Video

Updated: Jun 2, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

Backbone-driven collapse in unfolded protein chains.

Daniel P Teufel1, Christopher M Johnson, Jenifer K Lum

  • 1Medical Research Council Laboratory of Molecular Biology and Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, UK.

Journal of Molecular Biology
|April 19, 2011
PubMed
Summary
This summary is machine-generated.

Backbone hydrogen bonds, not side chains, drive protein collapse. This finding challenges hydrophobic theories and reveals how these interactions facilitate protein folding and the function of intrinsically disordered proteins.

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Microfluidic Mixers for Studying Protein Folding
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Microfluidic Mixers for Studying Protein Folding

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Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

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Related Experiment Videos

Last Updated: Jun 2, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

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

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Folding Dynamics

Background:

  • Protein collapse is a crucial early step in protein folding.
  • Intrinsically disordered proteins (IDPs) constitute a significant portion of the human proteome.
  • The driving forces behind protein collapse, particularly the roles of side-chain versus backbone interactions, remain debated.

Purpose of the Study:

  • To experimentally dissect the contributions of side-chain and backbone interactions to protein collapse.
  • To investigate the impact of these interactions on the structural properties and folding kinetics of intrinsically disordered proteins.
  • To resolve the controversy surrounding the role of backbone hydrogen bonds in protein folding.

Main Methods:

  • Utilized mutagenesis and chemical modification to alter specific interactions in disordered peptides and proteins.
  • Employed single-molecule fluorescence correlation spectroscopy to measure protein dimensions and intra-chain diffusion kinetics.
  • Avoided bulk measurement artifacts by focusing on individual polypeptide molecules.

Main Results:

  • Identified backbone interactions, not side chains, as the primary drivers of protein collapse into native-like globules.
  • Demonstrated that backbone hydrogen bonds significantly decrease polypeptide solubility and accelerate loop-closure kinetics.
  • Observed that side chains modulate domain dimensions and decelerate loop closure.

Conclusions:

  • Backbone interactions are sufficient to drive protein collapse, challenging the long-held hydrophobic hypothesis.
  • Transient backbone interactions facilitate the conformational search during early folding stages and within IDPs.
  • This study provides critical experimental evidence clarifying the roles of different molecular interactions in protein folding and IDP structure.