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Related Concept Videos

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 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

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Protein Folding01:22

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Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

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Related Experiment Video

Updated: May 18, 2026

4D Imaging of Protein Aggregation in Live Cells
08:59

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Published on: April 5, 2013

Myoglobin unfolding in crowding and confinement.

Ashima Malik1, Jayanta Kundu, Sanjib K Mukherjee

  • 1Department of Chemistry, Indian Institute of Technology Delhi, Hauz Khas, New Delhi.

The Journal of Physical Chemistry. B
|October 3, 2012
PubMed
Summary

Protein unfolding is destabilized by confinement in reverse micelles and some crowding agents, challenging common assumptions. Tryptophan lifetime may not reliably indicate protein structural changes.

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Last Updated: May 18, 2026

4D Imaging of Protein Aggregation in Live Cells
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Published on: April 5, 2013

Studying the Protein Quality Control System of D. discoideum Using Temperature-controlled Live Cell Imaging
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Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Area of Science:

  • Biophysics
  • Protein Chemistry
  • Macromolecular Crowding

Background:

  • Crowding and confinement are often conflated when studying protein structure and dynamics.
  • Macromolecular crowding agents are generally assumed to stabilize proteins.
  • Myoglobin (Mb) is a model protein for studying unfolding.

Purpose of the Study:

  • To investigate the unfolding of myoglobin (Mb) under confinement in AOT reverse micelles.
  • To examine the effects of common crowding agents (Ficoll 70, Dextran 70, Dextran 40) on Mb unfolding.
  • To assess the reliability of tryptophan (Trp)-heme distance as a probe for Mb structural changes.

Main Methods:

  • Studied Mb unfolding in AOT reverse micelle water pools.
  • Utilized macromolecular crowding agents: Ficoll 70, Dextran 70, and Dextran 40.
  • Performed tryptophan lifetime studies to probe protein structure.

Main Results:

  • Confinement in reverse micelles destabilized Mb, with distortion influenced by factors beyond cage size.
  • Crowding agents showed varied effects, with Ficoll 70 notably destabilizing Mb unfolding.
  • Tryptophan lifetime studies indicated that Trp-heme distance may not consistently reflect secondary structural changes in Mb.

Conclusions:

  • Confinement effects can be destabilizing for proteins like myoglobin, contrary to some expectations.
  • The stabilizing effect of macromolecular crowding agents is not universal; some can be destabilizing.
  • Tryptophan lifetime is not always a reliable indicator of secondary structure loss in myoglobin.