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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
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...
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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...
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...

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

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Protein crowding tunes protein stability.

Andrew C Miklos1, Mohona Sarkar, Yaqiang Wang

  • 1Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.

Journal of the American Chemical Society
|April 22, 2011
PubMed
Summary
This summary is machine-generated.

Cellular crowding by protein macromolecules can alter protein stability. Unlike synthetic polymers, protein crowders were found to be mildly destabilizing due to competing interactions, affecting protein function in biological systems.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Cellular environments are crowded, with macromolecules occupying up to 30% of cell volume.
  • Protein behavior in crowded conditions is predicted to differ significantly from dilute solutions.
  • Previous studies using synthetic polymers suggested crowding generally stabilizes proteins.

Purpose of the Study:

  • To investigate the impact of globular protein crowding on the thermodynamic stability of a small globular protein.
  • To compare the effects of protein-based crowders with synthetic polymer crowders.

Main Methods:

  • Quantification of equilibrium thermodynamic stability.
  • Use of globular proteins as crowders in a cellular milieu simulation.
  • Analysis of excluded-volume effects and nonspecific interactions.

Main Results:

  • Protein crowders exhibited a mild destabilizing effect on the target protein.
  • This effect resulted from a balance between stabilizing excluded-volume effects and destabilizing nonspecific interactions (e.g., electrostatic).
  • The interplay of these forces leads to tunable protein stability.

Conclusions:

  • Protein crowding can lead to destabilization, contrary to predictions based on synthetic crowders.
  • Nonspecific interactions play a crucial role in modulating protein stability in crowded biological environments.
  • Understanding these effects is vital for comprehending protein roles within living systems.