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PEDS Advance Access published online on September 9, 2005
Protein Engineering Design and Selection, doi:10.1093/protein/gzi056
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© The Author 2005. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org
Received February 15, 2005
Revised May 25, 2005
Accepted August 3, 2005

Article

Designability, aggregation propensity and duplication of disease-associated proteins

Philip Wong 1, Andreas Fritz 2, and Dmitrij Frishman 3*

1 Institute for Bioinformatics, GSF - National Research Center for Environment and Health, Ingolstädter Landstrasse 1, D-85764 Neuherberg, Germany
2 Biomax Informatics AG, Lochhamer Strasse 9, D-82152 Martinsried, Germany
3 Institute for Bioinformatics, GSF - National Research Center for Environment and Health, Ingolstädter Landstrasse 1, D-85764 Neuherberg, Germany; Department of Genome Oriented Bioinformatics, Technische Universität München, Wissenschaftzentrum Weihenstephan, D-85350 Freising, Germany

* To whom correspondence should be addressed.
Dmitrij Frishman, E-mail: d.frishman{at}wzw.tum.de


  Abstract

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.

Keywords: aggregation; designability; disease; duplication.
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