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

Huang, Renjie; Bonnichon, Arnaud; Claridge, Timothy DW; Leung, Ka Ho Ivanhoe

dc.contributor.author	Huang, Renjie	en
dc.contributor.author	Bonnichon, Arnaud	en
dc.contributor.author	Claridge, Timothy DW	en
dc.contributor.author	Leung, Ka Ho Ivanhoe	en
dc.date.accessioned	2018-11-19T01:46:56Z	en
dc.date.issued	2017-03-03	en
dc.identifier.citation	Scientific Reports 7:6 pages Article number 43727 03 Mar 2017	en
dc.identifier.issn	2045-2322	en
dc.identifier.uri	http://hdl.handle.net/2292/44456	en
dc.description.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.	en
dc.format.medium	Electronic	en
dc.language	eng	en
dc.relation.ispartofseries	Scientific reports	en
dc.rights	Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher.	en
dc.rights.uri	https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm	en
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	en
dc.subject	Humans	en
dc.subject	Caffeine	en
dc.subject	Tryptophan	en
dc.subject	Proteins	en
dc.subject	Serum Albumin	en
dc.subject	Ligands	en
dc.subject	Nuclear Magnetic Resonance, Biomolecular	en
dc.subject	Protein Binding	en
dc.subject	Kinetics	en
dc.title	Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding.	en
dc.type	Journal Article	en
dc.identifier.doi	10.1038/srep43727	en
pubs.begin-page	43727	en
pubs.volume	7	en
dc.rights.holder	Copyright: The authors	en
dc.identifier.pmid	28256624	en
pubs.publication-status	Published	en
dc.rights.accessrights	http://purl.org/eprint/accessRights/OpenAccess	en
pubs.subtype	Research Support, Non-U.S. Gov't	en
pubs.subtype	research-article	en
pubs.subtype	Journal Article	en
pubs.elements-id	615859	en
pubs.org-id	Science	en
pubs.org-id	Chemistry	en
dc.identifier.eissn	2045-2322	en
pubs.record-created-at-source-date	2017-03-04	en
pubs.dimensions-id	28256624	en