Prediction of Residue-specific Contributions to Binding and Thermal Stability Using Yeast Surface Display.
free energy
mutational scanning
protein stability
residue burial
saturation mutagenesis
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2021
2021
Historique:
received:
24
10
2021
accepted:
14
12
2021
entrez:
7
2
2022
pubmed:
8
2
2022
medline:
8
2
2022
Statut:
epublish
Résumé
Accurate prediction of residue burial as well as quantitative prediction of residue-specific contributions to protein stability and activity is challenging, especially in the absence of experimental structural information. This is important for prediction and understanding of disease causing mutations, and for protein stabilization and design. Using yeast surface display of a saturation mutagenesis library of the bacterial toxin CcdB, we probe the relationship between ligand binding and expression level of displayed protein, with
Identifiants
pubmed: 35127820
doi: 10.3389/fmolb.2021.800819
pii: 800819
pmc: PMC8814602
doi:
Types de publication
Journal Article
Langues
eng
Pagination
800819Informations de copyright
Copyright © 2022 Ahmed, Bhasin, Manjunath and Varadarajan.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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