Strategies for measurements of pseudocontact shifts in protein NMR spectroscopy
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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.author | John, Michael | |
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dc.contributor.author | Otting, Gottfried | |
dc.date.accessioned | 2015-12-10T21:54:01Z | |
dc.identifier.issn | 1439-4235 | |
dc.identifier.uri | http://hdl.handle.net/1885/38756 | |
dc.description.abstract | 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. This article discusses different approaches for pairwise resonance assignments, with emphasis on a strategy which exploits chemical exchange between the two states. | |
dc.publisher | Wiley-VCH Verlag GMBH | |
dc.source | ChemPhysChem | |
dc.subject | Keywords: 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.title | Strategies for measurements of pseudocontact shifts in protein NMR spectroscopy | |
dc.type | Journal article | |
local.description.notes | Imported from ARIES | |
local.identifier.citationvolume | 8 | |
dc.date.issued | 2007 | |
local.identifier.absfor | 069999 - Biological Sciences not elsewhere classified | |
local.identifier.ariespublication | u4005981xPUB166 | |
local.type.status | Published Version | |
local.contributor.affiliation | John, Michael, University of Gottingen | |
local.contributor.affiliation | Otting, Gottfried, College of Physical and Mathematical Sciences, ANU | |
local.description.embargo | 2037-12-31 | |
local.bibliographicCitation.issue | 16 | |
local.bibliographicCitation.startpage | 2309 | |
local.bibliographicCitation.lastpage | 2313 | |
local.identifier.doi | 10.1002/cphc.200700510 | |
dc.date.updated | 2015-12-09T07:23:01Z | |
local.identifier.scopusID | 2-s2.0-36549057912 | |
Collections | ANU Research Publications |
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