Fold Designability, Distribution, and Disease
Author Information
Author(s): Wong Philip, Frishman Dmitrij
Primary Institution: Institute for Bioinformatics, GSF–National Research Center for Environment and Health, Neuherberg, Germany
Hypothesis
Proteins with higher designability are more widespread and associated with fewer disease-related mutations.
Conclusion
The study suggests that folds with more families are more prevalent in proteomes and that many disease-related proteins have folds with fewer families.
Supporting Evidence
- Folds with more families are more sequence divergent.
- Many disease-related proteins have folds with fewer families.
- Designability is associated with the frequency of disease-related mutations.
Takeaway
Some proteins are built in a way that makes them stronger and more flexible, while others are more fragile and can lead to diseases when they change.
Methodology
The study used the SCOP database to estimate protein designability based on family counts within folds and compared these with disease associations.
Potential Biases
The classification of folds may be biased due to the manual nature of the SCOP database.
Limitations
The analysis is limited by the number of proteins with known SCOP folds and potential biases in disease data.
Statistical Information
P-Value
p<0.01
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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