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

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

doi:10.1039/c1cc11893e

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

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

Research output: Contribution to journal › Article › peer-review

43 Citations (Scopus)

Abstract

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 pseudocontact shifts and residual dipolar couplings in the NMR spectrum.

Original language	English
Pages (from-to)	7368-7370
Number of pages	3
Journal	Chemical Communications
Volume	47
Issue number	26
DOIs	https://doi.org/10.1039/c1cc11893e
Publication status	Published - 14 Jul 2011

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abstract = "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 pseudocontact shifts and residual dipolar couplings in the NMR spectrum.",

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AU - Swarbrick, James D.

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AU - Su, Xun Cheng

AU - Maleckis, Ansis

AU - Chhabra, Sandeep

AU - Huber, Thomas

AU - Otting, Gottfried

AU - Graham, Bim

PY - 2011/7/14

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AB - 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 pseudocontact shifts and residual dipolar couplings in the NMR spectrum.

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

Abstract

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