High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
Abstract Four novel 5D (HACA(N)CONH, HNCOCACB, (HACA)CON(CA)CONH, (H)NCO(NCA)CONH), and one 6D ((H)NCO(N)CACONH) NMR pulse sequences are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in indirectly detected dimensions. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel pulse sequences were successfully tested using δ subunit (20 kDa) of Bacillus subtilis RNA polymerase...
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02-21-2012 03:40 AM
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Bioorg Med Chem. 2011 Aug 27;
Authors: Masuda Y, Fukuchi M, Yatagawa T, Tada M, Takeda K, Irie K, Akagi KI, Monobe Y, Imazawa T, Takegoshi K
Abstract
Aggregation of 42-residue amyloid ?-protein (A?42) plays a pivotal role in the etiology of Alzheimer's disease (AD). Curcumin, the yellow pigment in the rhizome of turmeric, attracts...
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09-20-2011 03:10 PM
Sensitive 13Câ??13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields
Sensitive 13Câ??13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields
Abstract Sensitive 2D solid-state 13Câ??13C correlation spectra of amyloid β fibrils have been recorded at very fast spinning frequencies and very high magnetic fields. It is demonstrated that PARIS-xy recoupling using moderate rf amplitudes can provide structural information by promoting efficient magnetization transfer even under such challenging experimental conditions. Furthermore, it has been shown both experimentally and by numerical simulations that the method is not...
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04-01-2011 09:23 AM
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
J Am Chem Soc. 2010 Oct 6;132(39):13765-75
Authors: Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Böckmann A, Meier BH
We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal prion HET-s...
[NMR paper] High-resolution molecular structure of a peptide in an amyloid fibril determined by m
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.
Related Articles High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.
Proc Natl Acad Sci U S A. 2004 Jan 20;101(3):711-6
Authors: Jaroniec CP, MacPhee CE, Bajaj VS, McMahon MT, Dobson CM, Griffin RG
Amyloid fibrils are self-assembled filamentous structures associated with protein deposition conditions including Alzheimer's disease and the transmissible...
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11-24-2010 09:25 PM
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by So
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy
He?le?ne Van Melckebeke, Christian Wasmer, Adam Lange, Eiso AB, Antoine Loquet, Anja Bo?ckmann and Beat H. Meier
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja104213j/aop/images/medium/ja-2010-04213j_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja104213j
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qGRhA6CtOVc
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09-10-2010 12:48 AM
High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation an
High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure .
Related Articles High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure .
Biochemistry. 2010 Aug 13;
Authors: Bayro MJ, Maly T, Birkett NR, Macphee CE, Dobson CM, Griffin RG
The SH3 domain of the PI3 kinase (PI3-SH3 or PI3K-SH3) readily aggregates into fibrils in vitro and has served as an important model system in the...
High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation an
Biochemistry, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable). 
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