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

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Published on: April 28, 2011

Protein folding under confinement: a role for solvent.

Del Lucent1, V Vishal, Vijay S Pande

  • 1Biophysics Program, Stanford University, Stanford, CA 94305, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 15, 2007
PubMed
Summary

Spatial confinement impacts protein folding. Confining only the protein aids folding, but confining both protein and solvent alters protein folding dynamics and thermodynamics, creating a distinct unfolded state.

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Area of Science:

  • Biophysics
  • Computational Biology
  • Biochemistry

Background:

  • Protein folding studies typically occur in vitro, but in vivo environments present spatial confinement.
  • The effects of confinement on protein folding dynamics and thermodynamics are not fully understood.

Purpose of the Study:

  • To investigate the folding dynamics of villin, a small, fast-folding protein, under varying spatial confinement conditions.
  • To elucidate the impact of confining both protein and solvent on protein folding.

Main Methods:

  • Simulations of villin folding within an inert nanopore with explicit solvent.
  • Calculation of the probability of folding before unfolding (Pfold) under different confinement regimes.
  • Analysis of Pfold correlations to understand competing folding effects.

Main Results:

  • Confining only the protein destabilizes the unfolded state, promoting folding.
  • Confining both protein and solvent induces a solvent-mediated effect that destabilizes the native state.
  • Unfolding in confined protein-solvent systems leads to a compact unfolded state distinct from the bulk unfolded state.

Conclusions:

  • Solvent confinement significantly influences protein folding kinetics and thermodynamics.
  • These findings have implications for understanding protein folding within cellular environments, such as chaperonin cavities.