Installation of a rigid EDTA-like motif into a protein ?-helix for paramagnetic NMR spectroscopy with Co(II) ions.
Chemistry. 2015 Dec 4;
Authors: Swarbrick J, Ung P, Dennis M, Lee M, Chhabra S, Graham B
Abstract
Coupling two copies of an iminodiacetic acid-cysteine hybrid ligand to a pair of cysteine residues positioned in an i, i + 4 arrangement within a protein ?-helix leads to generation of an EDTA-like metal ion-binding motif. Rigid binding of a Co(II) ion by this motif produces pseudo-contact shifts suitable for paramagnetic NMR structural studies.
PMID: 26634335 [PubMed - as supplied by publisher]
[NMR paper] Recent Progresses in Studying Helix-helix Interactions in Proteins by Incorporating the Wenxiang Diagram into the NMR Spectroscopy.
Recent Progresses in Studying Helix-helix Interactions in Proteins by Incorporating the Wenxiang Diagram into the NMR Spectroscopy.
Related Articles Recent Progresses in Studying Helix-helix Interactions in Proteins by Incorporating the Wenxiang Diagram into the NMR Spectroscopy.
Curr Top Med Chem. 2015 Aug 18;
Authors: Zhou GP, Chen D, Liao S, Sun L, Huang RB
Abstract
All residues in an alpha helix can be characterized and dispositioned on a 2D the wenxiang diagram, which possesses the following features: (1) the relative...
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08-20-2015 07:36 PM
The application of paramagnetic lanthanoid ions in NMR spectroscopy on proteins
The application of paramagnetic lanthanoid ions in NMR spectroscopy on proteins
Publication date: Available online 4 November 2013
Source:Coordination Chemistry Reviews</br>
Author(s): Wei-Min Liu , Mark Overhand , Marcellus Ubbink</br>
Lanthanoids are gaining popularity as paramagnetic centers for high resolution nuclear magnetic resonance (NMR) spectroscopy. They provide valuable angular and long-distance restraints for structure calculations of proteins and protein complexes. The introduction of lanthanoids into a protein sample is complicated by the many...
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11-05-2013 06:34 AM
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 215</br>
Claudio Luchinat, Malini Nagulapalli, Giacomo Parigi, Luca Sgheri</br>
Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively placed...
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03-09-2012 09:16 AM
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 30 December 2011</br>
Claudio*Luchinat, Malini*Nagulapalli, Giacomo*Parigi, Luca*Sgheri</br>
Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively...
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12-31-2011 10:40 AM
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] Structural characterization of proteins with an attached ATCUN motif by paramagnetic
Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy.
Related Articles Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy.
J Am Chem Soc. 2001 Oct 10;123(40):9843-7
Authors: Donaldson LW, Skrynnikov NR, Choy WY, Muhandiram DR, Sarkar B, Forman-Kay JD, Kay LE
The use of a short, three-residue Cu(2+)-binding sequence, the ATCUN motif, is presented as an approach for extracting long-range distance...
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11-19-2010 08:44 PM
[NMR paper] NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking t
NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains.
Related Articles NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains.
J Mol Biol. 2001 Sep 7;312(1):167-75
Authors: Hanaoka S, Nagadoi A, Yoshimura S, Aimoto S, Li B, de Lange T, Nishimura Y
Mammalian telomeres are composed of long tandem arrays of double-stranded telomeric TTAGGG repeats associated with...
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11-19-2010 08:44 PM
[NMR paper] The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
Biochemistry. 1997 Nov 4;36(44):13657-66
Authors: Wang G, Sparrow JT, Cushley RJ
The conformation of a synthetic peptide of 46 residues from apoA-I was investigated by fluorescence, CD, and 2D NMR spectroscopies in lipid-mimetic environments....