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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
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Related Experiment Video

Updated: Jun 20, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Understanding protein folding cooperativity based on topological consideration.

L Wu1, W F Li, F Liu

  • 1Department of Physics and National Laboratory of Solid State Microstructure, Nanjing University, Nanjing 210093, China.

The Journal of Chemical Physics
|August 21, 2009
PubMed
Summary

Protein folding cooperativity is influenced by native topology. Key topological factors like scattered contacts and loop entropy differences correlate with protein folding types, impacting folding dynamics.

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Last Updated: Jun 20, 2026

Microfluidic Mixers for Studying Protein Folding
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Published on: April 10, 2012

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Area of Science:

  • Computational Biology
  • Protein Dynamics
  • Biophysics

Background:

  • Protein folding cooperativity is crucial for understanding protein folding dynamics.
  • Native protein topology significantly influences folding behavior and cooperativity.

Purpose of the Study:

  • To investigate the relationship between protein topology and folding cooperativity.
  • To identify key topological factors governing protein folding types.

Main Methods:

  • Simulations of proteins Naf-BBL, QNND-BBL, CI2, and SH3 using the Gō model.
  • Analysis of thermodynamic and kinetic coupling in protein folding.
  • Evaluation of topological features such as contact order and residue coupling.

Main Results:

  • Weak thermodynamic coupling between nonlocal native contacts observed in Naf-BBL.
  • Identified fraction of scattered native contacts, loop entropy differences, and long-range relative contact order as major topological factors.
  • These factors show significant correlation with different protein folding types (two-state and multistate).

Conclusions:

  • Protein tertiary structure plays a generic role in determining folding cooperativity.
  • Specific topological features dictate the folding behavior and cooperativity of proteins.
  • Understanding these topological origins provides insights into barrierless and downhill folding.