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

ABSTRACT: WaterLOGSY is a popular ligand-observed NMR technique to screen for protein-ligand interactions, yet when applied to measure dissociation constants (KD) through ligand titration, the results were found to be strongly dependent on sample conditions. Herein, we show that accurate KDs can be obtained by waterLOGSY with optimised experimental setup.

SUBMITTER: Huang R 

PROVIDER: S-EPMC5335602 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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

Huang Renjie R   Bonnichon Arnaud A   Claridge Timothy D W TD   Leung Ivanhoe K H IK  

Scientific reports 20170303

WaterLOGSY is a popular ligand-observed NMR technique to screen for protein-ligand interactions, yet when applied to measure dissociation constants (K<sub>D</sub>) through ligand titration, the results were found to be strongly dependent on sample conditions. Herein, we show that accurate K<sub>D</sub>s can be obtained by waterLOGSY with optimised experimental setup. ...[more]

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