NMR Applications for Identifying β-TrCP Protein-Ligand Interactions

Autor:	V. Tanchou, Julien Pons, J.-P. Girault, N. Evrard-Todeschi, G. Bertho
Rok vydání:	2011
Předmět:	Pharmacology Dissociation constant Crystallography Chemistry Drug Discovery Molecule Crystallographic data General Medicine Magnetization transfer Ligand (biochemistry) Protein ligand
Zdroj:	Mini-Reviews in Medicinal Chemistry. 11:283-297
ISSN:	1389-5575
DOI:	10.2174/138955711795305344
Popis:	In the absence of crystallographic data, NMR has emerged as the best way to define protein-ligand interactions. Using NMR experiments based on magnetization transfer, one can sort bound from unbound molecules, estimate the dissociation constant, identify contacts implied in the binding, characterize the structure of the bound ligand and conduct ligand competition assays.
Databáze:	OpenAIRE
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