title: Solubis: optimize your protein.
abstract: BACKGROUND
  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: VIB Switch Laboratory, Department of Cellular and Molecular Medicine, Katholieke Universiteit Leuven, 3000 Leuven, Belgium and Vrije Universiteit Brussel, 1050 Brussels, Belgium.
authors: Greet
authors: G
authors: De Baets
authors: VIB Switch Laboratory, Department of Cellular and Molecular Medicine, Katholieke Universiteit Leuven, 3000 Leuven, Belgium and Vrije Universiteit Brussel, 1050 Brussels, Belgium.
authors: Joost
authors: J
authors: Van Durme
authors: VIB Switch Laboratory, Department of Cellular and Molecular Medicine, Katholieke Universiteit Leuven, 3000 Leuven, Belgium and.
authors: Rob
authors: R
authors: van der Kant
authors: VIB Switch Laboratory, Department of Cellular and Molecular Medicine, Katholieke Universiteit Leuven, 3000 Leuven, Belgium and.
authors: Joost
authors: J
authors: Schymkowitz
authors: VIB Switch Laboratory, Department of Cellular and Molecular Medicine, Katholieke Universiteit Leuven, 3000 Leuven, Belgium and.
authors: Frederic
authors: F
authors: Rousseau
mesh_terms: D030562:Databases, Protein; D006801:Humans; D009154:Mutation / Q000235:genetics*; D011487:Protein Conformation; D017510:Protein Folding; D055503:Protein Multimerization; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D020539:Sequence Analysis, Protein / Q000379:methods*; D012984:Software; D013816:Thermodynamics
chemical_list: D011506:Proteins