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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.
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1038/srep43727

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Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Department:
Green Templeton College
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Funding agency for:
Bonnichon, A
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Publisher:
Nature Publishing Group Publisher's website
Journal:
Scientific Reports Journal website
Volume:
7
Issue:
43727
Pages:
1-6
Publication date:
2017-03-03
Acceptance date:
2017-01-27
DOI:
ISSN:
2045-2322
Pubs id:
pubs:685359
URN:
uri:a3e87038-d2f6-43d0-90ee-c0bf4ed7c2c6
UUID:
uuid:a3e87038-d2f6-43d0-90ee-c0bf4ed7c2c6
Local pid:
pubs:685359
Language:
English
Keywords:

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