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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: Jul 19, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Protein folding is slaved to solvent motions.

H Frauenfelder1, P W Fenimore, G Chen

  • 1Theory Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. frauenfelder@lanl.gov

Proceedings of the National Academy of Sciences of the United States of America
|October 13, 2006
PubMed
Summary

Protein folding rates are controlled by solvent alpha-fluctuations, a process termed slaving. This model explains folding speed by linking it to solvent dynamics and protein conformational substates.

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Microfluidic Mixers for Studying Protein Folding
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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

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Area of Science:

  • Biophysics
  • Protein Dynamics
  • Chemical Kinetics

Background:

  • Proteins fold from amino acid chains into functional structures.
  • Folding times vary significantly, from microseconds to hours.
  • The precise control mechanisms governing protein folding rates remain debated.

Purpose of the Study:

  • To propose a model for protein folding rates based on solvent dynamics.
  • To investigate the role of alpha-fluctuations in protein folding.
  • To explain the observed slowness of protein folding compared to solvent fluctuations.

Main Methods:

  • Postulating a 'slaving' model where protein motions are dictated by solvent fluctuations.
  • Applying the slaving concept to both folded protein motions and the folding process itself.
  • Analyzing the temperature dependence and rate coefficients of folding and solvent fluctuations.

Main Results:

  • Protein folding exhibits the same temperature dependence as solvent alpha-fluctuations but proceeds much slower.
  • The slaving model suggests folding rate is governed by solvent dynamics (k(alpha)) and the number of protein conformational substates.
  • Activation enthalpy of folding is primarily influenced by the solvent.

Conclusions:

  • Protein folding is a 'slaved' process, where conformational changes are controlled by solvent dynamics.
  • The folding rate (k(f)) is significantly slower than solvent fluctuations (k(alpha)) due to the vast number of accessible unfolded protein substates.
  • Beta-fluctuations may influence late stages of protein folding.