Fully Automated Characterization of Protein-Peptide Binding by Microfluidic 2D NMR.
Journal
Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056
Informations de publication
Date de publication:
08 02 2023
08 02 2023
Historique:
pubmed:
31
1
2023
medline:
10
2
2023
entrez:
30
1
2023
Statut:
ppublish
Résumé
We demonstrate an automated microfluidic nuclear magnetic resonance (NMR) system that quantitatively characterizes protein-ligand interactions without user intervention and with minimal sample needs through protein-detected heteronuclear 2D NMR spectroscopy. Quantitation of protein-ligand interactions is of fundamental importance to the understanding of signaling and other life processes. As is well-known, NMR provides rich information both on the thermodynamics of binding and on the binding site. However, the required titrations are laborious and tend to require large amounts of sample, which are not always available. The present work shows how the analytical power of NMR detection can be brought in line with the trend of miniaturization and automation in life science workflows.
Identifiants
pubmed: 36716203
doi: 10.1021/jacs.2c13052
pmc: PMC9912330
doi:
Substances chimiques
Ligands
0
Proteins
0
Peptides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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