Solubis: optimize your protein.

Abstract

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.

• Authors: Greet De Baets, Joost Van Durme, Rob van der Kant, Joost Schymkowitz, Frederic Rousseau
• Journal: Bioinformatics (Oxford, England) (Bioinformatics) Vol. 31 Issue 15 Pg. 2580-2 (Aug 01 2015) ISSN: 1367-4811 [Electronic] England
• PMID: 25792555 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: © The Author 2015. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: [email protected].

Chemical References

• Proteins

Topics

• Databases, Protein
• Humans
• Mutation (genetics)
• Protein Conformation
• Protein Folding
• Protein Multimerization
• Protein Stability
• Proteins (chemistry, genetics, metabolism)
• Sequence Analysis, Protein (methods)
• Software
• Thermodynamics