AGGRESCAN3D: Toward the prediction of the aggregation propensities of protein structures

Jordi Pujols, Samuel Peña-Díaz, Salvador Ventura

Research output: Chapter in BookChapterResearchpeer-review

5 Citations (Scopus)

Abstract

© 2018, Springer Science+Business Media, LLC, part of Springer Nature. Protein aggregation is responsible for the onset and spread of many human diseases, ranging from neurodegenerative disorders to cancer and diabetes. Moreover, it is one of the major bottlenecks for the production of protein-based therapeutics such as antibodies or enzymes. AGGRESCAN3D (A3D) is a web server aimed to identify and evaluate structural aggregation prone regions, overcoming the limitations of sequence-based algorithms in the prediction of the aggregation propensity of globular proteins. A3D allows the redesign of protein solubility by predicting in silico the impact of mutations and protein conformational fluctuations on the aggregation of native polypeptides.
Original languageEnglish
Title of host publicationMethods in Molecular Biology
Pages427-443
Number of pages16
Volume1762
DOIs
Publication statusPublished - 1 Jan 2018

Keywords

  • 3D structure
  • AGGRESCAN3D
  • Bioinformatics
  • Protein aggregation
  • Protein misfolding
  • Protein production
  • Protein solubility

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