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Solubis: optimize your protein

Journal Contribution - Journal Article

MOTIVATION: Protein aggregation is associated with a number of protein misfolding diseases and is a major concern for therapeutic proteins. Aggregation is caused by the presence of aggregation-prone regions (APRs) in the amino acid sequence of the protein. The lower the aggregation propensity of APRs and the better they are protected by native interactions within the folded structure of the protein, the more aggregation is prevented. Therefore, both the local thermodynamic stability of APRs in the native structure and their intrinsic aggregation propensity are a key parameter that needs to be optimized to prevent protein aggregation. RESULTS: The Solubis method presented here automates the process of carefully selecting point mutations that minimize the intrinsic aggregation propensity while improving local protein stability.
Journal: Bioinformatics
ISSN: 1367-4803
Issue: 15
Volume: 31
Pages: 2580 - 2582
Publication year:2015
BOF-keylabel:yes
IOF-keylabel:yes
BOF-publication weight:10
CSS-citation score:1
Authors from:Higher Education
Accessibility:Open