Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding

WaterLOGSY is a popular ligand-observed NMR technique to screen for protein-ligand interactions, yet when applied to measure dissociation constants (K(D)) through ligand titration, the results were found to be strongly dependent on sample conditions. Herein, we show that accurate K(D)s can be obtain...

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Detalles Bibliográficos
Autores principales: Huang, Renjie, Bonnichon, Arnaud, Claridge, Timothy D. W., Leung, Ivanhoe K. H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5335602/
https://www.ncbi.nlm.nih.gov/pubmed/28256624
http://dx.doi.org/10.1038/srep43727
Descripción
Sumario:WaterLOGSY is a popular ligand-observed NMR technique to screen for protein-ligand interactions, yet when applied to measure dissociation constants (K(D)) through ligand titration, the results were found to be strongly dependent on sample conditions. Herein, we show that accurate K(D)s can be obtained by waterLOGSY with optimised experimental setup.

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