Alzheimer fibrils at atomic resolution: Fundamental structural ... - Science Daily More...
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Magic-angle-spinning NMR used to probe protein/microtubule assembly at atomic scale - UD Daily
Magic-angle-spinning NMR used to probe protein/microtubule assembly at atomic scale - UD Daily
http://www.bionmr.com//t0.gstatic.com/images?q=tbn:ANd9GcT-781wgiL25Wj4lXbDk7r_19UWHOVZ3lHSUaO48tGMGj-ld0mE1LSgPhYcTamEvpxJ90b_7RGo
UD Daily
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Magic-angle-spinning NMR used to probe protein/microtubule assembly at atomic scale
UD Daily
5:30 p.m., Nov. 24, 2015--A latticework of tiny tubes called microtubules gives your cells their shape and also acts like a railroad track that essential proteins travel on. But if there is a glitch in the connection between...
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07-18-2016 03:40 AM
[NMR paper] Structural Polymorphism of Alzheimer's ?-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
Structural Polymorphism of Alzheimer's ?-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
Structural Polymorphism of Alzheimer's ?-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
J Am Chem Soc. 2016 Jul 14;
Authors: Elkins MR, Wang T, Nick M, Jo H, Lemmin T, Prusiner SB, DeGrado WF, Stoehr J, Hong M
Abstract
The amyloid-? (A?) peptide of the Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer scale and molecular scale. Various fibril growth conditions have been...
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07-16-2016 04:54 AM
Study reveals insights into protein linked to cancer, Alzheimer's disease - Science Daily
Study reveals insights into protein linked to cancer, Alzheimer's disease - Science Daily
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Study reveals insights into protein linked to cancer, Alzheimer's disease
Science Daily
NMR-based model for Pin1 (â??Aâ?? and â??Bâ?? globular domains), and its interaction with its â??disorderedâ?? protein targets pertinent to cancer and Alzheimer's disease (green). The Pin1 â??Aâ?? and â??Bâ?? domains specialize in peptidyl-prolyl isomerase activity and ...
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nmrlearner
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06-05-2016 02:18 AM
[NMR paper] High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
High Resolution Structural Characterization of A?42 Amyloid Fibrils by MAS NMR.
J Am Chem Soc. 2015 May 22;
Authors: Colvin MT, Silvers R, Frohm B, Su Y, Linse S, Griffin RG
Abstract
The presence of amyloid plaques composed of amyloid beta (A?) fibrils is a hallmark of Alzheimer's disease (AD). The A? peptide is present as several length variants with two common alloforms consisting of 40 and 42 amino acids, denoted A?1-40 and A?1-42, respectively....
Protein 'Filmed' While Unfolding at Atomic Resolution - Science Daily (press release)
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Protein 'Filmed' While Unfolding at Atomic Resolution
Science Daily (press release)
We hoped that these quantities would be sufficient to examine the intermediate forms with nuclear magnetic resonance (NMR) spectroscopy," said Markus Zweckstetter, head of the research groups "Protein Structure Determination using MNR" at the MPIbpc ...
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Protein 'Filmed' While Unfolding at Atomic Resolution - Science Daily (press release)
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nmrlearner
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02-11-2013 09:29 PM
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...
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01-21-2011 12:00 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