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Related Concept Videos

Protein Folding01:22

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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. 
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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.
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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.
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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: Thickening the broth.

A P Minton1

  • 1Building 8, Room 226, NIH, Bethesda, 20892-0830, USA. minton@helix.nih.gov

Current Biology : CB
|February 19, 2000
PubMed
Summary

Macromolecular crowding accelerates protein aggregation and hinders proper protein folding. This occurs due to kinetic competition between different processes influenced by crowding.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Macromolecular crowding is a ubiquitous phenomenon in biological systems.
  • Cellular environments are densely packed with macromolecules, influencing molecular interactions.
  • Understanding crowding effects is crucial for comprehending cellular processes.

Purpose of the Study:

  • To investigate the impact of macromolecular crowding on protein aggregation.
  • To explore the relationship between crowding, protein folding, and aggregation kinetics.
  • To provide a kinetic framework for understanding crowding-induced effects.

Main Methods:

  • Utilizing biophysical techniques to monitor protein folding and aggregation.
  • Employing kinetic modeling to analyze the influence of crowding on distinct processes.

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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
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  • Comparing aggregation rates under varying crowding conditions.

    • Main Results:

    • Macromolecular crowding significantly enhances the rate of protein aggregation.
    • Crowding disfavors correct protein folding, promoting aggregation pathways.
    • Kinetic analysis reveals competition between folding and aggregation influenced by crowding.

    Conclusions:

    • Macromolecular crowding promotes protein aggregation over correct folding.
    • The observed effects can be explained by the differential impact of crowding on competing kinetic processes.
    • This provides a mechanistic understanding of crowding's role in protein homeostasis and disease.