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Related Concept Videos

Protein Folding01:25

Protein Folding

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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.
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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Overview
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Molecular Chaperones and Protein Folding03:00

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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.
The...
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Amyloid Fibrils03:03

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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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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Related Experiment Video

Updated: Feb 27, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

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Cyclodextrins as protein folding aids

N Karuppiah1, A Sharma

  • 1Department of Chemistry, Central Michigan University, Mt. Pleasant 48859, USA.

Biochemical and Biophysical Research Communications
|June 6, 1995
PubMed
Summary
This summary is machine-generated.

Cyclodextrins prevent protein aggregation during carbonic anhydrase refolding. This method recovers over 90% of active enzyme, even at high concentrations, by binding to hydrophobic sites.

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Area of Science:

  • Biochemistry
  • Protein Folding
  • Enzymology

Background:

  • Protein aggregation is a common challenge during refolding from random coil to native structure.
  • Understanding factors that prevent aggregation is crucial for protein stability and function.

Purpose of the Study:

  • To investigate the effect of cyclodextrins on the refolding of carbonic anhydrase under conditions that promote aggregation.
  • To determine if cyclodextrins can enhance enzyme recovery and activity.

Main Methods:

  • Studied the refolding of carbonic anhydrase in the presence of cyclodextrins.
  • Assessed protein aggregation formation during renaturation.
  • Quantified the recovery of active enzyme at various protein concentrations.

Main Results:

  • Cyclodextrins effectively prevented the formation of protein aggregates during carbonic anhydrase renaturation.
  • Over 90% of active enzyme was recovered, even at high protein concentrations (up to 67 microM).

Conclusions:

  • Cyclodextrins are effective in preventing protein aggregation during refolding.
  • The mechanism likely involves cyclodextrins binding to hydrophobic sites on folding intermediates.
  • This approach significantly enhances protein reactivation and enzyme recovery.