Structural Insights into How Protein Environments Tune the Spectroscopic Properties of a Noncanonical Amino Acid Fluorophore.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
22 09 2020
22 09 2020
Historique:
pubmed:
28
8
2020
medline:
17
3
2021
entrez:
27
8
2020
Statut:
ppublish
Résumé
Genetically encoded fluorescent noncanonical amino acids (fNCAAs) could be used to develop novel fluorescent sensors of protein function. Previous efforts toward this goal have been limited by the lack of extensive physicochemical and structural characterizations of protein-based sensors containing fNCAAs. Here, we report the steady-state spectroscopic properties and first structural analyses of an fNCAA-containing Fab fragment of the 5c8 antibody, which binds human CD40L. A previously reported 5c8 variant in which the light chain residue Ile
Identifiants
pubmed: 32845612
doi: 10.1021/acs.biochem.0c00474
pmc: PMC7964926
mid: NIHMS1674420
doi:
Substances chimiques
Amino Acids
0
Fluorescent Dyes
0
Immunoglobulin Fab Fragments
0
CD40 Ligand
147205-72-9
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
3401-3410Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM103393
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM136996
Pays : United States
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