Solubis: optimize your protein | Zendy

Greet De Baets | Zendy; Joost Van Durme | Zendy; Rob van der Kant | Zendy; Joost Schymkowitz | Zendy; Frédéric Rousseau | Zendy

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Solubis: optimize your protein

Author(s) -

Greet De Baets,

Joost Van Durme,

Rob van der Kant,

Joost Schymkowitz,

Frédéric Rousseau

Publication year - 2015

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/btv162

Subject(s) - computer science , protein aggregation , protein stability , sequence (biology) , protein folding , data aggregator , process (computing) , stability (learning theory) , computational biology , chemistry , biology , genetics , machine learning , programming language , biochemistry , computer network , wireless sensor network

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.

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