The New Functional Hybrid Chaperone Protein ADGroEL-SacSm.
chaperone
domain rearrangement
hybrid protein
protein engineering
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
23 Aug 2023
23 Aug 2023
Historique:
received:
14
07
2023
revised:
20
08
2023
accepted:
21
08
2023
medline:
11
9
2023
pubmed:
9
9
2023
entrez:
9
9
2023
Statut:
epublish
Résumé
The creation of new proteins by combining natural domains is a commonly used technique in protein engineering. In this work, we have tested the possibilities and limitations of using circular homo-oligomeric Sm-like proteins as a basis for attaching other domains. Attachment to such a stable base should bring target domains together and keep them in the correct mutual orientation. We chose a circular homoheptameric Sm-like protein from
Identifiants
pubmed: 37687025
pii: molecules28176196
doi: 10.3390/molecules28176196
pmc: PMC10488932
pii:
doi:
Substances chimiques
Molecular Chaperones
0
Chaperonin 60
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Russian Science Foundation
ID : 22-24-00934
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