Structural Robustness Affects the Engineerability of Aminoacyl-tRNA Synthetases for Genetic Code Expansion.
Amino Acids
/ genetics
Amino Acyl-tRNA Synthetases
/ chemistry
Catalytic Domain
/ genetics
Escherichia coli
/ genetics
Escherichia coli Proteins
/ genetics
Genetic Code
/ genetics
Protein Engineering
/ methods
RNA, Transfer
/ metabolism
Substrate Specificity
/ genetics
Tyrosine-tRNA Ligase
/ chemistry
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
23 02 2021
23 02 2021
Historique:
pubmed:
10
2
2021
medline:
12
6
2021
entrez:
9
2
2021
Statut:
ppublish
Résumé
The ability to engineer the substrate specificity of natural aminoacyl-tRNA synthetase/tRNA pairs facilitates the site-specific incorporation of noncanonical amino acids (ncAAs) into proteins. The
Identifiants
pubmed: 33560840
doi: 10.1021/acs.biochem.1c00056
pmc: PMC8004357
mid: NIHMS1683514
doi:
Substances chimiques
Amino Acids
0
Escherichia coli Proteins
0
RNA, Transfer
9014-25-9
Amino Acyl-tRNA Synthetases
EC 6.1.1.-
Tyrosine-tRNA Ligase
EC 6.1.1.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
489-493Subventions
Organisme : NIAAA NIH HHS
ID : R21 AA015398
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM136437
Pays : United States
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