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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 Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

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Related Experiment Video

Updated: Jun 8, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Is protein folding sub-diffusive?

Sergei V Krivov1

  • 1Institute of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom. s.krivov@leeds.ac.uk

Plos Computational Biology
|September 24, 2010
PubMed
Summary

Protein folding dynamics can appear sub-diffusive due to suboptimal reaction coordinates. Using the optimal coordinate reveals diffusive protein folding dynamics on the free energy surface.

Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Dynamics

Background:

  • Protein folding is often modeled as diffusive motion on a free energy landscape.
  • Recent studies indicate protein dynamics projected onto reaction coordinates are frequently sub-diffusive.
  • This challenges the adequacy of conventional diffusive models.

Purpose of the Study:

  • To investigate the relationship between reaction coordinate choice and observed protein dynamics.
  • To determine if optimal reaction coordinates reveal diffusive folding dynamics.
  • To understand why sub-diffusive dynamics are often observed.

Main Methods:

  • Numerical construction of an optimal reaction coordinate for a protein folding trajectory.
  • Analysis of protein dynamics projected onto both optimal and sub-optimal reaction coordinates.

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

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Last Updated: Jun 8, 2026

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Published on: April 10, 2012

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08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

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  • Correlation of free energy profile height with dynamics diffusion characteristics.

    • Main Results:

    • Dynamics projected onto the optimal reaction coordinate exhibited diffusive behavior.
    • Dynamics projected onto sub-optimal coordinates showed sub-diffusive behavior.
    • Higher free energy profiles correlated with more diffusive projected dynamics.

    Conclusions:

    • The observed diffusion or sub-diffusion of protein dynamics is dependent on the chosen reaction coordinate.
    • Protein folding can be accurately described as diffusion on the free energy surface using an optimal reaction coordinate.
    • Commonly used, intuitive reaction coordinates are often sub-optimal, leading to observed sub-diffusive dynamics.