Designability, aggregation propensity and duplication of disease-associated proteins

Philip Wong, Andreas Fritz, Dmitrij Frishman

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Over 2000 proteins in the Ensembl human genome database have been linked with disease information from OMIM. In comparison with all human proteins, we find that disease-associated proteins tend to have less designable folds in terms of their SCOP family counts, suggesting that they are intrinsically less robust to mutation and environmental stress. Disease proteins also tend to have isoelectric points closer to neutrality and more alternating hydrophilic-hydrophobic amino acid stretches compared with the average human protein. These results suggest that protein aggregation is a significant phenomenon associated with diseases. Another finding in this work is that many disease proteins are highly sequence similar to other disease proteins, suggesting that gene duplication has contributed to the expansion of disease-prone protein families.

Original languageEnglish
Pages (from-to)503-508
Number of pages6
JournalProtein Engineering, Design and Selection
Issue number10
StatePublished - Oct 2005
Externally publishedYes


  • Aggregation
  • Designability
  • Disease
  • Duplication


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