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

Autor:	Huang R; School of Chemical Sciences, The University of Auckland, Private Bag 92019, Victoria Street West, Auckland 1142, New Zealand., Bonnichon A; Department of Chemistry, University of Oxford, Chemistry Research Laboratory, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.; Université D'Auvergne, 49 Boulevard François-Mitterrand, CS 60032, Clermont Ferrand 63001, Cedex 1, France., Claridge TD; Department of Chemistry, University of Oxford, Chemistry Research Laboratory, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom., Leung IK; School of Chemical Sciences, The University of Auckland, Private Bag 92019, Victoria Street West, Auckland 1142, New Zealand.
Jazyk:	angličtina
Zdroj:	Scientific reports [Sci Rep] 2017 Mar 03; Vol. 7, pp. 43727. Date of Electronic Publication: 2017 Mar 03.
DOI:	10.1038/srep43727
Abstrakt:	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.
Databáze:	MEDLINE
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