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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...
Protein Organization01:13

Protein Organization

Overview

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Related Experiment Video

Updated: Jun 4, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

How does the first water shell fold proteins so fast?

Olivier Collet1

  • 1Institut Jean Lamour, Département 1, CNRS, Nancy-Université, UPV-Metz, Vandoeuvre-lès-Nancy, France. olivier.collet@ijl.nancy-universite.fr

The Journal of Chemical Physics
|March 3, 2011
PubMed
Summary

Protein folding dynamics are significantly influenced by water

Area of Science:

  • Protein dynamics
  • Biophysics
  • Statistical mechanics

Background:

  • Protein folding is essential for biological function.
  • The role of solvent, particularly water, is critical in protein dynamics.
  • Understanding protein-solvent interactions is key to deciphering folding mechanisms.

Purpose of the Study:

  • To investigate the role of water in protein folding dynamics.
  • To explore the influence of hydration shells and bulk solvent on protein conformational changes.
  • To elucidate the mechanism of protein folding influenced by solvent properties.

Main Methods:

  • Utilized a theoretical protein-solvent model.
  • Employed a statistical physics approach.
  • Simulated protein chain folding using master-equation evolution.

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Related Experiment Videos

Last Updated: Jun 4, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

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

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Main Results:

  • Identified a double-funnel mechanism governing protein folding.
  • Observed rapid folding into native structures above glass-transition temperature via pathways with broken hydrogen bonds.
  • Found that below glass-transition temperature, pathways with formed hydrogen bonds dominate, but with longer relaxation times.

Conclusions:

  • Protein folding dynamics are dictated by a dual mechanism involving solvent interactions.
  • The interplay between hydrogen bond formation/breaking in water and protein conformation is crucial.
  • Solvent-driven pathways, even if transient, significantly impact folding rates and mechanisms.