Related ArticlesModeling an in-register, parallel "iowa" a? fibril structure using solid-state NMR data from labeled samples with rosetta.
Structure. 2015 Jan 6;23(1):216-27
Authors: Sgourakis NG, Yau WM, Qiang W
Abstract
Determining the structures of amyloid fibrils is an important first step toward understanding the molecular basis of neurodegenerative diseases. For ?-amyloid (A?) fibrils, conventional solid-state NMR structure determination using uniform labeling is limited by extensive peak overlap. We describe the characterization of a distinct structural polymorph of A? using solid-state NMR, transmission electron microscopy (TEM), and Rosetta model building. First, the overall fibril arrangement is established using mass-per-length measurements from TEM. Then, the fibril backbone arrangement, stacking registry, and "steric zipper" core interactions are determined using a number of solid-state NMR techniques on sparsely (13)C-labeled samples. Finally, we perform Rosetta structure calculations with an explicitly symmetric representation of the system. We demonstrate the power of the hybrid Rosetta/NMR approach by modeling the in-register, parallel "Iowa" mutant (D23N) at high resolution (1.2Å backbone rmsd). The final models are validated using an independent set of NMR experiments that confirm key features.
[NMR paper] Site-Specific Solid-State NMR Studies of "Trigger Factor" in Complex with the Large Ribosomal Subunit 50S.
Site-Specific Solid-State NMR Studies of "Trigger Factor" in Complex with the Large Ribosomal Subunit 50S.
Related Articles Site-Specific Solid-State NMR Studies of "Trigger Factor" in Complex with the Large Ribosomal Subunit 50S.
Angew Chem Int Ed Engl. 2015 Feb 5;
Authors: Barbet-Massin E, Huang CT, Daebel V, Hsu ST, Reif B
Abstract
Co-translational protein folding is not yet well understood despite the availability of high-resolution ribosome crystal structures. We present first solid-state NMR data on non-mobile regions of a...
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02-08-2015 01:21 AM
Postdoctoral position "DNP-enhanced bio solid-state NMR"
Postdoctoral position "DNP-enhanced bio solid-state NMR"
One of the most demanding challenges of biomolecular NMR spectroscopy is the inherently low sensitivity. Signal enhancement by DNP is therefore a promising ...
blog.bridge12.com/.../postdoctoral-position-dnp-enhanced-bio...
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06-09-2013 03:14 AM
Postdoctoral position "DNP-enhanced bio solid-state NMR"
From The DNP-NMR Blog:
Postdoctoral position "DNP-enhanced bio solid-state NMR"
A postdoc position for “DNP-enhanced solid-state NMR” will be available from September 2013 at the Helmholtz center Jülich/ Heinrich Heine-Universität Düsseldorf.
One of the most demanding challenges of biomolecular NMR spectroscopy is the inherently low sensitivity. Signal enhancement by DNP is therefore a promising alternative to gain insights into systems which otherwise could not be investigated. We will exploit the technique to obtain structural information on complex systems (protein aggregates,...
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06-05-2013 06:53 PM
Structure determination in "shiftless" solid state NMR of oriented protein samples.
Structure determination in "shiftless" solid state NMR of oriented protein samples.
Structure determination in "shiftless" solid state NMR of oriented protein samples.
J Magn Reson. 2011 Jul 6;
Authors: Yin Y, Nevzorov AA
An efficient formalism for calculating protein structures from oriented-sample NMR data in the torsion-angle space is presented. Angular anisotropies of the NMR observables are treated by utilizing an irreducible spherical basis of rotations. An intermediate rotational transformation is introduced that greatly speeds up...
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07-12-2011 06:23 PM
NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Dismutase.
NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Dismutase.
NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Dismutase.
J Am Chem Soc. 2010 Dec 16;
Authors: Banci L, Bertini I, Blaževitš O, Cantini F, Lelli M, Luchinat C, Mao J, Vieru M
Demetalated superoxide dismutase (SOD1) is a transient species, fibrillogenic in nature and of biomedical interest. It is a conformationally disordered protein difficult to characterize. We have developed a strategy based on the NMR investigation...
Cannot processe T1 data..."no region specific for intrng"?!
When I was processing data for T1/T2 analysis (from t1ir), it appears the error messengers "No region specific for intrng" but I have already followed the guide to define ranges.....And there is also no integration data in final report, just show "eliminated". Please help me:( THANK YOU SO MUCH :)