Related ArticlesSolid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Chembiochem. 2005 Sep;6(9):1679-84
Authors: Hiller M, Krabben L, Vinothkumar KR, Castellani F, van Rossum BJ, Kühlbrandt W, Oschkinat H
Uniformly 13C-,15N-labelled outer-membrane protein G (OmpG) from Escherichia coli was expressed for structural studies by solid-state magic-angle spinning (MAS) NMR. Inclusion bodies of the recombinant, labelled protein were purified under denaturing conditions and refolded in detergent. OmpG was reconstituted into lipid bilayers and several milligrams of two-dimensional crystals were obtained. Solid-state MAS NMR spectra showed signals with an apparent line width of 80-120 Hz (including homonuclear scalar couplings). Signal patterns for several amino acids, including threonines, prolines and serines were resolved and identified in 2D proton-driven spin-diffusion (PDSD) spectra.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
Riqiang Fu, Xingsheng Wang, Conggang Li, Adriana N. Santiago-Miranda, Gary J. Pielak and Fang Tian
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja204062v/aop/images/medium/ja-2011-04062v_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja204062v
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/BuOPwKpaHdw
[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.
Related Articles Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.
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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[NMR paper] Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
Related Articles Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
J Am Chem Soc. 2005 Sep 21;127(37):12965-74
Authors: Andronesi OC, Becker S, Seidel K, Heise H, Young HS, Baldus M
It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments...
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[NMR paper] Magic angle spinning solid-state NMR spectroscopy for structural studies of protein i
Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
Related Articles Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
J Am Chem Soc. 2004 Dec 22;126(50):16608-20
Authors: Marulanda D, Tasayco ML, McDermott A, Cataldi M, Arriaran V,...
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11-24-2010 10:03 PM
[NMR paper] Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscop
Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.
Related Articles Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.
Nature. 2002 Nov 7;420(6911):98-102
Authors: Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H
The determination of a representative set of protein structures is a chief aim in structural genomics. Solid-state NMR may have a crucial role in structural investigations of those proteins that do not easily form crystals or are not...
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11-24-2010 08:58 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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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...
Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
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