Magic Angle Spinning NMR of Proteins: High-Frequency Dynamic Nuclear Polarization and (1)H Detection.
Annu Rev Biochem. 2015 Mar 30;
Authors: Su Y, Andreas L, Griffin RG
Abstract
Magic angle spinning (MAS) NMR studies of amyloid and membrane proteins and large macromolecular complexes are an important new approach to structural biology. However, the applicability of these experiments, which are based on (13)C- and (15)N-detected spectra, would be enhanced if the sensitivity were improved. Here we discuss two advances that address this problem: high-frequency dynamic nuclear polarization (DNP) and (1)H-detected MAS techniques. DNP is a sensitivity enhancement technique that transfers the high polarization of exogenous unpaired electrons to nuclear spins via microwave irradiation of electron-nuclear transitions. DNP boosts NMR signal intensities by factors of 10(2) to 10(3), thereby overcoming NMR's inherent low sensitivity. Alternatively, it permits structural investigations at the nanomolar scale. In addition, (1)H detection is feasible primarily because of the development of MAS rotors that spin at frequencies of 40 to 60 kHz or higher and the preparation of extensively (2)H-labeled proteins. Expected final online publication date for the Annual Review of Biochemistry Volume 84 is June 02, 2015. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.
PMID: 25839340 [PubMed - as supplied by publisher]
Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins
Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins
Abstract
Heteronucleus-detected dipolar based correlation spectroscopy is established for assignments of 1H, 13C, and 15N resonances and structural analysis in fully protonated proteins. We demonstrate that 13C detected 3D experiments are highly efficient and permit assignments of the majority of backbone resonances, as shown in an 89-residue dynein light chain 8, LC8 protein. With these experiments, we...
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[NMR paper] Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.
Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.
Related Articles Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.
J Biomol NMR. 2014 Nov 9;
Authors: Guo C, Hou G, Lu X, O'Hare B, Struppe J, Polenova T
Abstract
Heteronucleus-detected dipolar based correlation spectroscopy is established for assignments of (1)H, (13)C, and (15)N...
Solid state nuclear magnetic resonance with magic-angle spinning and dynamic nuclear polarization below 25K
Solid state nuclear magnetic resonance with magic-angle spinning and dynamic nuclear polarization below 25K
January 2013
Publication year: 2013
Source:Journal of Magnetic Resonance, Volume 226</br>
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We describe an apparatus for solid state nuclear magnetic resonance (NMR) with dynamic nuclear polarization (DNP) and magic-angle spinning (MAS) at 20–25K and 9.4Tesla. The MAS NMR probe uses helium to cool the sample space and nitrogen gas for MAS drive and bearings, as described earlier , but also includes a corrugated waveguide for transmission of microwaves from...
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12-15-2012 09:51 AM
Solid state nuclear magnetic resonance with magic-angle spinning and dynamic nuclear polarization below 25 K
Solid state nuclear magnetic resonance with magic-angle spinning and dynamic nuclear polarization below 25 K
Available online 20 November 2012
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
</br>
We describe an apparatus for solid state nuclear magnetic resonance (NMR) with dynamic nuclear polarization (DNP) and magic-angle spinning (MAS) at 20-25 K and 9.4 Tesla. The MAS NMR probe uses helium to cool the sample space and nitrogen gas for MAS drive and bearings, as described earlier (Thurber et al., J. Magn. Reson. 2008) , but also includes a...
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Solid state nuclear magnetic resonance with magic-angle spinning and dynamic nuclear polarization below 25 K
Solid state nuclear magnetic resonance with magic-angle spinning and dynamic nuclear polarization below 25 K
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Kent R. Thurber, Alexey Potapov, Wai-Ming Yau, Robert Tycko</br>
We describe an apparatus for solid state nuclear magnetic resonance (NMR) with dynamic nuclear polarization (DNP) and magic-angle spinning (MAS) at 20-25 K and 9.4 Tesla. The MAS NMR probe uses helium to cool the sample space and nitrogen gas for MAS drive and bearings, as described earlier (Thurber et al., J. Magn. Reson. 2008) ,...
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Intermolecular Structure Determination of Amyloid Fibrils with Magic-Angle Spinning and Dynamic Nuclear Polarization NMR
Intermolecular Structure Determination of Amyloid Fibrils with Magic-Angle Spinning and Dynamic Nuclear Polarization NMR
Marvin J. Bayro, Galia T. Debelouchina, Matthew T. Eddy, Neil R. Birkett, Catherine E. MacPhee, Melanie Rosay, Werner E. Maas, Christopher M. Dobson and Robert G. Griffin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203756x/aop/images/medium/ja-2011-03756x_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203756x
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.
Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.
Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.
J Am Chem Soc. 2011 Jul 21;
Authors: Bayro MJ, Debelouchina GT, Eddy MT, Birkett NR, Macphee CE, Rosay MM, Maas WE, Dobson CM, Griffin RG
We describe magic-angle spinning NMR experiments designed to elucidate the interstrand architecture of amyloid fibrils. Three methods are introduced for this purpose, two...