Related ArticlesNMR spectroscopic studies of I = 1/2 metal ions in biological systems.
Biochem Cell Biol. 1998;76(2-3):223-34
Authors: Oz G, Pountney DL, Armitage IM
This article reviews the use of nuclear magnetic resonance methods of spin 1/2 metal nuclei to probe the metal binding site(s) in a variety of metalloproteins. The majority of the studies have involved native Zn(II) and Ca(II) metalloproteins where there has been isostructural substitution of these metal ions with the I = 1/2 (111/113)Cd(II) ion. Also included are recent studies that have utilized the 109Ag(I) ion to probe Cu(I) sites in yeast metallothionein and 199Hg(II) as a probe of the metal binding sites in mercury resistance proteins. Pertinent aspects for the optimal execution of these experiments along with the procedures for the metal substitution reactions are discussed together with the presentation of a 113Cd chemical shift correlation map with ligand type and coordination number. Specific examples of protein systems studied using the (111/113)Cd and 109Ag nuclei include the metallothionein superfamily of Zn(II)- and Cu(I)-binding proteins from mammalian, invertebrate, and yeast systems. In addition to the structural features revealed by these metal ion nuclear magnetic resonance studies, important new information is frequently provided about the dynamics at the active-site metal ion. In an effort for completeness, other less frequently used spin 1/2 metal nuclei are mentioned.
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...
NMR studies of alkali metal ions in organic and biological solids
NMR studies of alkali metal ions in organic and biological solids
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 13 June 2011</br>
Gang, Wu , Jianfeng, Zhu</br>
*Highlights:*? Comprehensive review of NMR of alkali metal ions in organic/biological solids ? Experimental solid-state NMR techniques and computational methods ? Survey of experimental alkali metal NMR data for organic/biological solids</br></br>
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06-14-2011 02:30 AM
DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin
DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 10 March 2011</br>
Matthias J.N., Junk , Hans W., Spiess , Dariush, Hinderberger</br>
In this study, self-assembled systems of human serum albumin (HSA) and spin-labeled fatty acids are characterized by double electron–electron resonance (DEER). HSA, being the most important transport protein of the human blood, is capable to host up to seven paramagnetic fatty acid...
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03-11-2011 05:00 PM
1H NMR-based metabolic profiling reveals inherent biological variation in yeast and nematode model systems
1H NMR-based metabolic profiling reveals inherent biological variation in yeast and nematode model systems
Abstract The application of metabolomics to human and animal model systems is poised to provide great insight into our understanding of disease etiology and the metabolic changes that are associated with these conditions. However, metabolomic studies have also revealed that there is significant, inherent biological variation in human samples and even in samples from animal model systems where the animals are housed under carefully controlled conditions. This inherent biological...
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03-03-2011 02:06 AM
[NMR paper] An NMR method for studying the kinetics of metal exchange in biomolecular systems.
An NMR method for studying the kinetics of metal exchange in biomolecular systems.
Related Articles An NMR method for studying the kinetics of metal exchange in biomolecular systems.
J Biomol NMR. 2002 Aug;23(4):303-9
Authors: Barbieri R, Hore PJ, Luchina C, Pierattelli R
The kinetics of lanthanide (III) exchange for calcium(II) in the C-terminal EF-hand of the protein calbindin D9k have been studied by one-dimensional (1D) stopped-flow NMR. By choosing a paramagnetic lanthanide (Ce3+), kinetics in the sub-second range can be easily measured....
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11-24-2010 08:58 PM
23rd International Conference on Magnetic Resonance in Biological Systems
23rd International Conference on Magnetic Resonance in Biological Systems
Location: Sheraton San Diego Hotel & Marina, San Diego, California
Date: August 24-29, 2008
Important Dates & Deadlines:
Now! - Post-deadline abstract submissions will continue to be considered for poster presentations on a space available basis