Understanding Protein Folding and Misfolding
Author Information
Author(s): Stefani Massimo
Primary Institution: University of Florence, Florence, Italy
Hypothesis
The study explores the relationship between protein folding, misfolding, and aggregation, particularly focusing on the role of surfaces in these processes.
Conclusion
The findings suggest that surfaces can significantly influence protein folding and misfolding, impacting the formation of amyloid aggregates associated with various diseases.
Supporting Evidence
- Protein folding and aggregation are competing pathways relying on similar physicochemical principles.
- Surfaces can modify the path of protein misfolding and aggregation, generating different structures.
- Macromolecular crowding in cells can favor protein aggregation.
Takeaway
Proteins need to fold correctly to work properly, but sometimes they get mixed up and form clumps that can be harmful. Surfaces around them can help or hurt this process.
Methodology
The review discusses various experimental and theoretical approaches used to study protein folding and aggregation, including spectroscopic and simulation techniques.
Limitations
The review primarily focuses on in vitro studies, which may not fully replicate the complex intracellular environment.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website