Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins
Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins
Abstract Well-resolved 2Hâ??13C correlation spectra, reminiscent of 1Hâ??13C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane protein G (OmpG) from E. coli by exploiting the favorable lifetime of 2H double-quantum (DQ) states. Sufficient signal-to-noise was achieved due to the short deuterium T 1, allowing for high repetition rates and enabling 3D experiments with a 2Hâ??13C transfer step in a reasonable time....
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11-01-2011 01:52 AM
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
J Phys Chem Lett. 2011 Jul 21;2(14):1836-1841
Authors: Tang M, Berthold DA, Rienstra CM
Membrane proteins play an important role in many biological functions. Solid-state NMR spectroscopy is uniquely suited for studying structure and dynamics of membrane proteins in a membranous environment. The major challenge to obtain high quality solid-state NMR spectra of membrane proteins is...
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08-16-2011 01:19 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
J Am Chem Soc. 2011 Mar 1;
Authors: Renault M, Bos MP, Tommassen J, Baldus M
Multidomain proteins constitute a large part of prokaryotic and eukaryotic proteomes and play fundamental roles in various physiological processes. However, their structural characterization is challenging because of their large size and...
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03-03-2011 12:34 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Marie Renault, Martine P. Bos, Jan Tommassen and Marc Baldus
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109469c/aop/images/medium/ja-2010-09469c_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109469c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9XN1qiW-S-I
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03-02-2011 02:01 AM
[NMR paper] Characterization of protein-ligand interactions by high-resolution solid-state NMR sp
Characterization of protein-ligand interactions by high-resolution solid-state NMR spectroscopy.
Related Articles Characterization of protein-ligand interactions by high-resolution solid-state NMR spectroscopy.
J Am Chem Soc. 2004 Nov 3;126(43):13948-53
Authors: Zech SG, Olejniczak E, Hajduk P, Mack J, McDermott AE
A novel approach for detection of ligand binding to a protein in solid samples is described. Hydrated precipitates of the anti-apoptotic protein Bcl-xL show well-resolved (13)C-(13)C 2D solid-state NMR spectra that allow...
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11-24-2010 10:03 PM
[NMR paper] Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral
Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width.
Related Articles Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width.
J Magn Reson. 1999 Jan;136(1):86-91
Authors: Hong M
A technique for obtaining dipolar-mediated INADEQUATE NMR spectra with a large spectral window in the double-quantum dimension is presented. Using the dipolar recoupling sequence C7 to excite the double-quantum coherence under magic-angle spinning, the technique involves incrementing the...
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11-18-2010 07:05 PM
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Angew Chem Int Ed Engl. 2010 Jul 28;
Authors: Zhu J, Ye E, Terskikh V, Wu G
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08-17-2010 03:36 AM
Ligand-membrane protein binding by solid-state NMR
Selective Interface Detection: Mapping Binding Site Contacts in Membrane Proteins by NMR Spectroscopy
Suzanne R. Kiihne, Alain F. L. Creemers, Willem J. de Grip, Petra H. M. Bovee-Geurts, Johan Lugtenburg, and Huub J. M. de Groot
J. Am. Chem. Soc.; 2005; 127(16) pp 5734 - 5735
ABSTRACT:
Intermolecular contact surfaces are important regions where specific interactions mediate biological function. We introduce a new magic angle spinning solid state NMR technique, dubbed "selective interface detection spectroscopy" (SIDY). In this technique, 13C-attached protons (1Hlig) are dephased by...