What is the Difference Between Folded and Unfolded Protein?
🆚 Go to Comparative Table 🆚The main difference between folded and unfolded proteins lies in their structure and function. Here are the key differences:
- Structure: Folded proteins have a ordered, globular structure with a tightly packed hydrophobic core, while unfolded proteins have a disordered, open structure with loosely packed side chains.
- Function: Folded proteins are biologically active and function correctly, while unfolded proteins are biologically inactive and do not function correctly.
- Conformation: Folded proteins have a native three-dimensional structure, which is crucial for their function. Unfolded proteins, on the other hand, lack a stable three-dimensional structure.
- Plasticity: Unfolded proteins have a large plasticity, allowing them to interact efficiently with several different targets, as compared to a folded protein with limited conformational flexibility.
- Denaturation: Folded proteins can be converted into an unfolded state through denaturation, which involves extreme temperature, extreme pH, mechanical forces, and chemical denaturants.
In summary, folded proteins have a stable, ordered structure and are biologically active, while unfolded proteins have a disordered structure and are biologically inactive. Proteins must be correctly folded into specific, stable, three-dimensional conformations in order to function correctly.
Comparative Table: Folded vs Unfolded Protein
Here is a table comparing folded and unfolded proteins:
| Feature | Folded Protein | Unfolded Protein |
|---|---|---|
| Structure | Ordered, globular structure with a tightly packed hydrophobic core | Disordered, open structure |
| Biological Activity | Functions correctly and is biologically active | Does not function correctly and is biologically inactive |
| Protein Folding | Occurs in vivo as a protein is being made on a ribosome, often assisted by folding chaperones | Requires correct folding into stable three-dimensional conformations to become functional |
| Exposure of Hydrophobic Groups | Decreased exposure to water of apolar groups | Increased exposure to water of apolar groups |
| Aggregation | Less likely to aggregate with other proteins | More likely to aggregate with other proteins |
| Disease Impact | Unfolded proteins contribute to the pathology of many diseases | Folded proteins are essential for proper cellular function |
Folded proteins have a specific, stable, three-dimensional conformation, which is crucial for their biological function. Unfolded proteins, on the other hand, lack an ordered structure and must fold into stable conformations to become functional. Extreme temperature, extreme pH, mechanical forces, and chemical denaturants can convert folded proteins into unfolded states.
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- Protein Denaturation vs Hydrolysis
- Recombinant DNA vs Recombinant Protein
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