Dissimilarity in the Folding of Human Cytosolic Creatine Kinase Isoenzymes
2011
Folding Differences in Human Cytosolic Creatine Kinase Isoenzymes
publication
Evidence: moderate
Author Information
Author(s): Wang Yin, Wang Sha, Gao Yan-Song, Chen Zhe, Zhou Hai-Meng, Yan Yong-Bin
Primary Institution: Tsinghua University, Beijing, China
Hypothesis
The study investigates the role of N-terminal and C-terminal domains in the folding of human creatine kinase isoenzymes.
Conclusion
The study found that the domain interactions significantly influence the folding behavior and stability of creatine kinase isoenzymes.
Supporting Evidence
- The study demonstrated that the folding rates of creatine kinase isoenzymes vary significantly based on their domain interactions.
- Spectroscopic results indicated distinct structural features among the isoenzymes depending on their domain organizations.
- Fast folding of certain isoenzymes led to the accumulation of aggregation-prone intermediates.
Takeaway
This research looks at how different parts of a protein called creatine kinase help it fold properly, which is important for its function.
Methodology
The study compared the equilibrium and kinetic folding parameters of different creatine kinase isoenzymes using spectroscopic methods.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website