Current research on the role of copper in the conformational changes associated with prion diseases are reviewed with emphasis on the latest applications of NMR and EPR spectroscopy to probe the interactions of copper with prion proteins.
[NMR paper] Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.
Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.
Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.
Magn Reson Chem. 2013 Feb 24;
Authors: Emwas AH, Al-Talla ZA, Guo X, Al-Ghamdi S, Al-Masri HT
Abstract
Copper is an essential nutrient for the normal development of the brain and nervous system, although the hallmark of several neurological diseases is a change in copper concentrations in the brain and central nervous system. Prion protein (PrP) is a copper-binding,...
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02-26-2013 06:35 PM
Journal Highlight: How to tickle spins with a Fourier Transform NMR spectrometer
Journal Highlight: How to tickle spins with a Fourier Transform NMR spectrometer
http://www.spectroscopynow.com/common/images/thumbnails/13c920587a1.jpgSpin tickling can readily be achieved in homonuclear systems with Fourier transform NMR spectrometers by applying short pulses in the intervals between the sampling points.
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02-04-2013 08:00 PM
Journal Highlight: Determination of free fatty acids in edible oils by 1H NMR spectroscopy
Journal Highlight: Determination of free fatty acids in edible oils by 1H NMR spectroscopy
http://www.spectroscopynow.com/common/images/thumbnails/13c10b7ddda.jpgA novel proton NMR assay for the determination of free fatty acids in edible oils is a suitable alternative to the acid value method.
Source: Spectroscopynow.com
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02-03-2013 08:49 AM
Journal Highlight: Combined use of filtered and edited 1H NMR spectroscopy to detect 13C-enriched compounds in complex mixtures
Journal Highlight: Combined use of filtered and edited 1H NMR spectroscopy to detect 13C-enriched compounds in complex mixtures
http://www.spectroscopynow.com/common/images/thumbnails/13b5c5e9785.jpgThe 13C background signal can be distinguished from resonances of 13C-enriched xenobiotics by the absence of a 12C component, detected by combined analysis of 13C-filtered and -edited proton NMR spectra.
Source: Spectroscopynow.com
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02-03-2013 08:49 AM
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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09-20-2011 03:10 PM
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
Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation.
Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation.
Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation.
J Mol Biol. 2011 Aug 4;
Authors: Biljan I, Ilc G, Giachin G, Raspadori A, Zhukov I, Plavec J, Legname G
The development of transmissible spongiform encephalopathies (TSEs) is associated with the conversion of the cellular prion protein (PrP(C)) into a misfolded, pathogenic isoform (PrP(Sc)). Spontaneous generation...
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08-16-2011 01:19 PM
[NMR paper] Prion protein NMR structure and species barrier for prion diseases.
Prion protein NMR structure and species barrier for prion diseases.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Prion protein NMR structure and species barrier for prion diseases.
Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7281-5
Authors: Billeter M, Riek R, Wider G, Hornemann S, Glockshuber R, Wüthrich K
The structural...
Journal Highlight: Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases
Current research on the role of copper in the conformational changes associated with prion diseases are reviewed with emphasis on the latest applications of NMR and EPR spectroscopy to probe the interactions of copper with prion proteins.
Linear Mode
