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...
[NMR paper] Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.
Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.
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J Phys Chem B. 2005 Sep 29;109(38):18135-45
Authors: Marulanda D, Tasayco ML, Cataldi M, Arriaran V, Polenova T
De novo site-specific 13C and 15N backbone and sidechain resonance assignments are presented for uniformly enriched E. coli thioredoxin, established using...
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12-01-2010 06:56 PM
Automated protein resonance assignments of magic angle spinning solid-state NMR spect
Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of β1 immunoglobulin binding domain of protein G (GB1)
Abstract Magic-angle spinning solid-state NMR (MAS SSNMR) represents a fast developing experimental technique with great potential to provide structural and dynamics information for proteins not amenable to other methods. However, few automated analysis tools are currently available for MAS SSNMR. We present a methodology for automating protein resonance assignments of MAS SSNMR spectral data and its application to experimental peak lists of the...
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10-15-2010 05:16 PM
Automated protein resonance assignments of magic angle spinning solid-state NMR spect
Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of ?1 immunoglobulin binding domain of protein G (GB1).
Related Articles Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of ?1 immunoglobulin binding domain of protein G (GB1).
J Biomol NMR. 2010 Oct 8;
Authors: Moseley HN, Sperling LJ, Rienstra CM
Magic-angle spinning solid-state NMR (MAS SSNMR) represents a fast developing experimental technique with great potential to provide structural and dynamics information for...