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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
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...
Protein and Protein Structure02:15

Protein and Protein Structure

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 can...

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Related Experiment Video

Updated: May 27, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

How, when and why proteins collapse: the relation to folding.

Gilad Haran1

  • 1Chemical Physics Department, Weizmann Institute of Science, Rehovot 76100, Israel.

Current Opinion in Structural Biology
|November 23, 2011
PubMed
Summary

Unfolded proteins can collapse into compact states near native conditions, a fast transition driven by hydrophobic and backbone forces. This collapse facilitates protein folding by destabilizing the unfolded state.

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Last Updated: May 27, 2026

Microfluidic Mixers for Studying Protein Folding
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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Area of Science:

  • Biophysics
  • Protein dynamics
  • Chemical physics

Background:

  • Proteins exist in various states, from expanded unfolded forms to compact folded structures.
  • Understanding the transitions between these states is crucial for protein function and misfolding diseases.

Purpose of the Study:

  • To investigate the coil-globule transition in unfolded proteins.
  • To characterize the kinetics and driving forces of protein collapse.

Main Methods:

  • Single-molecule Förster Resonance Energy Transfer (FRET) experiments.
  • Time-resolved studies utilizing FRET and small-angle scattering.
  • Analysis of protein collapse under near-native conditions.

Main Results:

  • Unfolded proteins can adopt compact globular structures distinct from their folded states.
  • Protein collapse is a rapid event, occurring on the submicrosecond timescale.
  • Hydrophobic and backbone interactions are identified as key forces driving protein collapse.

Conclusions:

  • The coil-globule transition is a significant phenomenon for unfolded proteins.
  • Protein collapse destabilizes the unfolded state, promoting folding.
  • Natively unfolded proteins readily exhibit collapse behavior.