Automated optimization of the solubility of a hyper-stable α-amylase.


Journal

Open biology
ISSN: 2046-2441
Titre abrégé: Open Biol
Pays: England
ID NLM: 101580419

Informations de publication

Date de publication:
May 2024
Historique:
medline: 15 5 2024
pubmed: 15 5 2024
entrez: 15 5 2024
Statut: ppublish

Résumé

Most successes in computational protein engineering to date have focused on enhancing one biophysical trait, while multi-trait optimization remains a challenge. Different biophysical properties are often conflicting, as mutations that improve one tend to worsen the others. In this study, we explored the potential of an automated computational design strategy, called CamSol Combination, to optimize solubility and stability of enzymes without affecting their activity. Specifically, we focus on

Identifiants

pubmed: 38745462
doi: 10.1098/rsob.240014
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

240014

Subventions

Organisme : Royal Society
ID : URF\R1\201461

Auteurs

Montader Ali (M)

Yusuf Hamied Department of Chemistry, University of Cambridge , Cambridge CB2 1EW, UK.

Matthew Greenig (M)

Yusuf Hamied Department of Chemistry, University of Cambridge , Cambridge CB2 1EW, UK.

Marc Oeller (M)

Yusuf Hamied Department of Chemistry, University of Cambridge , Cambridge CB2 1EW, UK.
Proteomics and Signal Transduction, Max Planck Institute of Biochemistry , Martinsried 82152, Germany.

Misha Atkinson (M)

Yusuf Hamied Department of Chemistry, University of Cambridge , Cambridge CB2 1EW, UK.

Xing Xu (X)

Yusuf Hamied Department of Chemistry, University of Cambridge , Cambridge CB2 1EW, UK.

Pietro Sormanni (P)

Yusuf Hamied Department of Chemistry, University of Cambridge , Cambridge CB2 1EW, UK.

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Classifications MeSH