Journal
SCIENTIFIC REPORTS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep43727
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Funding
- Neurological Foundation of New Zealand
- Health Research Council of New Zealand
- University of Auckland
- Biochemical Society
- Le Conseil Regional d'Auvergne
- La Fondation d'Auvergne
- Erasmus Programme
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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.
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