Synergistic stabilization of a double mutant in chymotrypsin inhibitor 2 from a library screen in E. coli.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
18 08 2021
18 08 2021
Historique:
received:
28
04
2021
accepted:
26
07
2021
entrez:
19
8
2021
pubmed:
20
8
2021
medline:
15
12
2021
Statut:
epublish
Résumé
Most single point mutations destabilize folded proteins. Mutations that stabilize a protein typically only have a small effect and multiple mutations are often needed to substantially increase the stability. Multiple point mutations may act synergistically on the stability, and it is often not straightforward to predict their combined effect from the individual contributions. Here, we have applied an efficient in-cell assay in E. coli to select variants of the barley chymotrypsin inhibitor 2 with increased stability. We find two variants that are more than 3.8 kJ mol
Identifiants
pubmed: 34408246
doi: 10.1038/s42003-021-02490-7
pii: 10.1038/s42003-021-02490-7
pmc: PMC8373930
doi:
Substances chimiques
Peptides
0
Plant Proteins
0
chymotrypsin inhibitor 2
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
980Informations de copyright
© 2021. The Author(s).
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