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- W2740366956 endingPage "8101" @default.
- W2740366956 startingPage "8094" @default.
- W2740366956 abstract "Solid-state NMR is becoming a powerful tool to detect atomic-level structural features of biomolecules even when they are bound to (or trapped in) solid systems that lack long-range three-dimensional order. We here demonstrate that it is possible to probe protein–ligand interactions from a protein-based perspective also when the protein is entrapped in silica, thus translating into biomolecular solid-state NMR all of the considerations that are usually made to understand the chemical nature of the interaction of a protein with its ligands. This work provides a proof of concept that also immobilized enzymes can be used for protein-based NMR protein–ligand interactions for drug discovery." @default.
- W2740366956 created "2017-08-08" @default.
- W2740366956 creator A5025782742 @default.
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- W2740366956 creator A5069642187 @default.
- W2740366956 creator A5071760085 @default.
- W2740366956 creator A5072329968 @default.
- W2740366956 creator A5082753420 @default.
- W2740366956 date "2017-08-16" @default.
- W2740366956 modified "2023-09-27" @default.
- W2740366956 title "High-Resolution Solid-State NMR Characterization of Ligand Binding to a Protein Immobilized in a Silica Matrix" @default.
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