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Engineering of a bis-chelator motif into a protein α-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy

Swarbrick, James; Ung, Phuc; Su, Xun-Cheng; Maleckis, Ansis; Chhabra, Sandeep; Graham, Bim; Otting, Gottfried; Huber, Thomas

Description

Attachment of two nitrilotriacetic acid-based ligands to a protein α-helix in an i, i + 4 configuration produces an octadentate chelating motif that is able to bind paramagnetic lanthanide ions rigidly and with high affinity, leading to large pseudoconta

dc.contributor.authorSwarbrick, James
dc.contributor.authorUng, Phuc
dc.contributor.authorSu, Xun-Cheng
dc.contributor.authorMaleckis, Ansis
dc.contributor.authorChhabra, Sandeep
dc.contributor.authorGraham, Bim
dc.contributor.authorOtting, Gottfried
dc.contributor.authorHuber, Thomas
dc.date.accessioned2015-12-10T22:51:19Z
dc.identifier.issn1359-7345
dc.identifier.urihttp://hdl.handle.net/1885/58994
dc.description.abstractAttachment of two nitrilotriacetic acid-based ligands to a protein α-helix in an i, i + 4 configuration produces an octadentate chelating motif that is able to bind paramagnetic lanthanide ions rigidly and with high affinity, leading to large pseudoconta
dc.publisherRoyal Society of Chemistry
dc.sourceChemical Communications
dc.subjectKeywords: edetic acid; lanthanide; nitrilotriacetic acid; alpha helix; article; binding affinity; cross coupling reaction; ligand binding; nuclear magnetic resonance spectroscopy; protein binding; protein engineering; protein motif; protein protein interaction; Ami
dc.titleEngineering of a bis-chelator motif into a protein α-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume47
dc.date.issued2011
local.identifier.absfor060112 - Structural Biology (incl. Macromolecular Modelling)
local.identifier.absfor030503 - Organic Chemical Synthesis
local.identifier.absfor030606 - Structural Chemistry and Spectroscopy
local.identifier.ariespublicationu4005981xPUB468
local.type.statusPublished Version
local.contributor.affiliationSwarbrick, James, Monash University
local.contributor.affiliationUng, Phuc, Monash Institute of Pharmaceutical Sciences
local.contributor.affiliationSu, Xun-Cheng, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationMaleckis, Ansis, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationChhabra, Sandeep, Monash Institute of Pharmaceutical Sciences
local.contributor.affiliationHuber, Thomas, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationOtting, Gottfried, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationGraham, Bim, Monash University
local.description.embargo2037-12-31
local.bibliographicCitation.issue26
local.bibliographicCitation.startpage7368
local.bibliographicCitation.lastpage7370
local.identifier.doi10.1039/c1cc11893e
local.identifier.absseo860803 - Human Pharmaceutical Treatments (e.g. Antibiotics)
dc.date.updated2016-02-24T10:24:17Z
local.identifier.scopusID2-s2.0-79959383052
local.identifier.thomsonID000291823400020
CollectionsANU Research Publications

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