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Strategies for measurements of pseudocontact shifts in protein NMR spectroscopy

John, Michael; Otting, Gottfried

Description

Paramagnetic metal ions bound to proteins generate a dipolar field that can be accurately probed by pseudocontact shifts (PCS) displayed by the protein's nuclear spins. PCS are highly useful for determining the coordinates of individual spins in the molecule and for rapid structure determinations of entire protein-protein and protein-ligand complexes. However, PCS measurements require reliable resonance assignments for the molecule in its paramagnetic state and in a diamagnetic reference state....[Show more]

dc.contributor.authorJohn, Michael
dc.contributor.authorOtting, Gottfried
dc.date.accessioned2015-12-10T21:54:01Z
dc.identifier.issn1439-4235
dc.identifier.urihttp://hdl.handle.net/1885/38756
dc.description.abstractParamagnetic metal ions bound to proteins generate a dipolar field that can be accurately probed by pseudocontact shifts (PCS) displayed by the protein's nuclear spins. PCS are highly useful for determining the coordinates of individual spins in the molecule and for rapid structure determinations of entire protein-protein and protein-ligand complexes. However, PCS measurements require reliable resonance assignments for the molecule in its paramagnetic state and in a diamagnetic reference state. This article discusses different approaches for pairwise resonance assignments, with emphasis on a strategy which exploits chemical exchange between the two states.
dc.publisherWiley-VCH Verlag GMBH
dc.sourceChemPhysChem
dc.subjectKeywords: metalloprotein; protein; chemical structure; chemistry; methodology; nuclear magnetic resonance; review; Metalloproteins; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Proteins Chemical exchange; Metalloproteins; Paramagnetic relaxation enhancement; Pseudocontact shift; Resonance assignment
dc.titleStrategies for measurements of pseudocontact shifts in protein NMR spectroscopy
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume8
dc.date.issued2007
local.identifier.absfor069999 - Biological Sciences not elsewhere classified
local.identifier.ariespublicationu4005981xPUB166
local.type.statusPublished Version
local.contributor.affiliationJohn, Michael, University of Gottingen
local.contributor.affiliationOtting, Gottfried, College of Physical and Mathematical Sciences, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue16
local.bibliographicCitation.startpage2309
local.bibliographicCitation.lastpage2313
local.identifier.doi10.1002/cphc.200700510
dc.date.updated2015-12-09T07:23:01Z
local.identifier.scopusID2-s2.0-36549057912
CollectionsANU Research Publications

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