Related ArticlesA caged lanthanide complex as a paramagnetic shift agent for protein NMR.
Chemistry. 2004 Jul 5;10(13):3252-60
Authors: Prudêncio M, Rohovec J, Peters JA, Tocheva E, Boulanger MJ, Murphy ME, Hupkes HJ, Kosters W, Impagliazzo A, Ubbink M
A lanthanide complex, named CLaNP (caged lanthanide NMR probe) has been developed for the characterisation of proteins by paramagnetic NMR spectroscopy. The probe consists of a lanthanide chelated by a derivative of DTPA (diethylenetriaminepentaacetic acid) with two thiol reactive functional groups. The CLaNP molecule is attached to a protein by two engineered, surface-exposed, Cys residues in a bidentate manner. This drastically limits the dynamics of the metal relative to the protein and enables measurements of pseudocontact shifts. NMR spectroscopy experiments on a diamagnetic control and the crystal structure of the probe-protein complex demonstrate that the protein structure is not affected by probe attachment. The probe is able to induce pseudocontact shifts to at least 40 A from the metal and causes residual dipolar couplings due to alignment at a high magnetic field. The molecule exists in several isomeric forms with different paramagnetic tensors; this provides a fast way to obtain long-range distance restraints.
An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe.
An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe.
An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe.
J Biomol NMR. 2011 Sep 17;
Authors: Saio T, Ogura K, Shimizu K, Yokochi M, Burke TR, Inagaki F
Abstract
A nuclear magnetic resonance-based ligand screening strategy utilizing a paramagnetic lanthanide probe is presented. By fixing a paramagnetic lanthanide ion to a target protein, a pseudo-contact shift (PCS) and a paramagnetic relaxation...
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An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe
An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe
Abstract A nuclear magnetic resonance-based ligand screening strategy utilizing a paramagnetic lanthanide probe is presented. By fixing a paramagnetic lanthanide ion to a target protein, a pseudo-contact shift (PCS) and a paramagnetic relaxation enhancement (PRE) can be observed for both the target protein and its bound ligand. Based on PRE and PCS information, the bound ligand is then screened from the compound library and the structure of the ligandâ??protein complex is determined. PRE is an...
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09-20-2011 05:02 AM
An iminodiacetic acid based lanthanide binding tag for paramagnetic exchange NMR spectroscopy.
An iminodiacetic acid based lanthanide binding tag for paramagnetic exchange NMR spectroscopy.
An iminodiacetic acid based lanthanide binding tag for paramagnetic exchange NMR spectroscopy.
Angew Chem Int Ed Engl. 2011 May 2;50(19):4403-6
Authors: Swarbrick JD, Ung P, Chhabra S, Graham B
PMID: 21480444
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08-19-2011 02:56 PM
Engineering of a bis-chelator motif into a protein ?-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy.
Engineering of a bis-chelator motif into a protein ?-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy.
Engineering of a bis-chelator motif into a protein ?-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy.
Chem Commun (Camb). 2011 May 27;
Authors: Swarbrick JD, Ung P, Su XC, Maleckis A, Chhabra S, Huber T, Otting G, Graham B
Attachment of two nitrilotriacetic acid-based ligands to a protein ?-helix in an i, i + 4 configuration produces an octadentate chelating motif that is able to bind paramagnetic...
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05-28-2011 06:50 PM
[NMR paper] Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and it
Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and its application to elucidate long distance information.
Related Articles Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and its application to elucidate long distance information.
FEBS Lett. 2004 May 21;566(1-3):157-61
Authors: Nomura M, Kobayashi T, Kohno T, Fujiwara K, Tenno T, Shirakawa M, Ishizaki I, Yamamoto K, Matsuyama T, Mishima M, Kojima C
The paramagnetic metal chelate complex Cu(2+)-iminodiacetic acid (Cu(2+)-IDA) was...
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11-24-2010 09:51 PM
NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived fr
NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx.
Related Articles NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx.
Biomol NMR Assign. 2010 Oct 7;
Authors: Naik MT, Chang CC, Naik NM, Kung CC, Shih HM, Huang TH
Small Ubiquitin-like MOdifiers (SUMOs) are ubiquitin-like proteins known to covalently modify large number of cellular proteins. The mammalian SUMO family includes four paralogues, SUMO-1 through SUMO-4....
[NMR paper] Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
Biochemistry. 1997 May 27;36(21):6326-35
Authors: Ubbink M, Bendall DS
The complexes of horse ferrous and ferric cytochrome c with Cd-substituted pea plastocyanin have been characterized by nuclear magnetic resonance, in order to determine the binding sites and to study...
A caged lanthanide complex as a paramagnetic shift agent for protein NMR.
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