Researchers in the USA have used solid-state nuclear magnetic resonance (NMR) spectroscopy to study the rogue proteins involved in familial human cerebral amyloid angiopathy (CAA). This hereditary neurodegenerative condition is one of the family of prion diseases that afflict mammals and include bovine spongiform encephalopathy (often referred to colloquially as "mad cow disease"), Creutzfeldt-Jakob disease in humans, their equivalents in cats, mice, hamsters and other animals.
[NMR paper] Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
Nat Commun. 2017 Sep 29;8(1):753
Authors: Theint T, Nadaud PS, Aucoin D, Helmus JJ, Pondaven SP, Surewicz K, Surewicz WK, Jaroniec CP
Abstract
One of the most puzzling aspects of the prion diseases is the intricate relationship between prion strains and interspecies transmissibility barriers....
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10-01-2017 09:32 PM
[NMR paper] Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations.
Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations.
J Phys Chem B. 2015 Sep 10;119(36):11998-2006
Authors: Karki I, Wang H, Geise NR, Wilson BW, Lewis JP, Gullion T
Abstract
...
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06-14-2016 08:23 PM
[NMR Sparky Yahoo group] Can't pick peaks using restricted peak pick
Can't pick peaks using restricted peak pick
Hi all, I'm new to sparky and I'm using HSQC, HNcoCACB and HNCACB to do backbone assignments. I selected all picks in the HSQC and used it to find peaks in
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06-29-2013 11:49 AM
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion
Abstract We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly 13C, 15N labeled protein sample, sequential chemical-shift information for 74% of the N, Cα, Cβ triples, and for 80% of further side-chain resonances for these spin systems. We describe the procedures and protocols devised, and discuss possibilities and limitations of the...
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08-04-2011 01:14 AM
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
J Biomol NMR. 2011 Jul 31;
Authors: Habenstein B, Wasmer C, Bousset L, Sourigues Y, Schütz A, Loquet A, Meier BH, Melki R, Böckmann A
We present the de novo resonance assignments for the crystalline 33*kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly (13)C, (15)N labeled...
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08-02-2011 11:40 AM
[NMR paper] High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloi
High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
Related Articles High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
Angew Chem Int Ed Engl. 2005 Apr 15;44(16):2441-4
Authors: Siemer AB, Ritter C, Ernst M, Riek R, Meier BH
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11-25-2010 08:21 PM
[NMR paper] Solid-state NMR studies of the secondary structure of a mutant prion protein fragment
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Related Articles Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11686-90
Authors: Laws DD, Bitter HM, Liu K, Ball HL, Kaneko K, Wille H, Cohen FE, Prusiner SB, Pines A, Wemmer DE
The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89-143), was studied in...
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11-19-2010 08:44 PM
[NMR paper] Solid-state NMR studies of the prion protein H1 fragment.
Solid-state NMR studies of the prion protein H1 fragment.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solid-state NMR studies of the prion protein H1 fragment.
Protein Sci. 1996 Aug;5(8):1655-61
Authors: Heller J, Kolbert AC, Larsen R, Ernst M, Bekker T, Baldwin M, Prusiner SB, Pines A, Wemmer DE
Conformational...
Pick up a prion: Solid state NMR spots the differences
Researchers in the USA have used solid-state nuclear magnetic resonance (NMR) spectroscopy to study the rogue proteins involved in familial human cerebral amyloid angiopathy (CAA). This hereditary neurodegenerative condition is one of the family of prion diseases that afflict mammals and include bovine spongiform encephalopathy (often referred to colloquially as "mad cow disease"), Creutzfeldt-Jakob disease in humans, their equivalents in cats, mice, hamsters and other animals.
Linear Mode
