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Experimental NMR techniques for studies of protein-ligand interactions

dc.contributor.authorOtting, Gottfrieden
dc.date.accessioned2026-03-23T01:40:34Z
dc.date.available2026-03-23T01:40:34Z
dc.date.issued1993en
dc.description.abstractNMR studies of protein-ligand interactions range from using NMR as a tool with which to monitor ligand binding to the determination of the three-dimensional structure of complexes at atomic resolution. In recent years, selective and uniform enrichment with stable isotopes has promoted the investigation of ever larger systems at increasing resolution, and significant advances have been made using NMR techniques that focus specifically on the interaction of proteins and ligands.en
dc.description.statusPeer-revieweden
dc.format.extent9en
dc.identifier.issn0959-440Xen
dc.identifier.otherORCID:/0000-0002-0563-0146/work/209074904en
dc.identifier.scopus0027361390en
dc.identifier.urihttps://hdl.handle.net/1885/733807647
dc.language.isoenen
dc.sourceCurrent Opinion in Structural Biologyen
dc.titleExperimental NMR techniques for studies of protein-ligand interactionsen
dc.typeJournal articleen
dspace.entity.typePublicationen
local.bibliographicCitation.lastpage768en
local.bibliographicCitation.startpage760en
local.contributor.affiliationOtting, Gottfried; Karolinska Instituteten
local.identifier.citationvolume3en
local.identifier.doi10.1016/0959-440X(93)90061-Oen
local.identifier.pure993b5c00-9aad-4495-a8f3-23b0492260cben
local.identifier.urlhttps://www.scopus.com/pages/publications/0027361390en
local.type.statusPublisheden

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