Learning about protein solubility from bacterial inclusion bodies
2009
Understanding Protein Solubility in Bacteria
Commentary
Evidence: moderate
Author Information
Author(s): Martínez-Alonso Mónica, González-Montalbán Nuria, García-Fruitós Elena, Villaverde Antonio
Primary Institution: Institute for Biotechnology and Biomedicine, Autonomous University of Barcelona
Hypothesis
The belief that soluble proteins are always properly folded and functional is being challenged by new research.
Conclusion
Current research indicates that soluble proteins in bacteria may not be as functionally reliable as previously thought.
Supporting Evidence
- Soluble proteins can be misfolded and inactive.
- Inclusion bodies can contain functional proteins.
- Temperature and chaperone availability affect protein quality.
- Functional proteins can be extracted from inclusion bodies without denaturation.
Takeaway
Scientists are learning that just because a protein is soluble doesn't mean it's working properly. Sometimes, proteins that clump together can actually be useful.
Digital Object Identifier (DOI)
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