Related ArticlesProbing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures with different uniform labeling.
J Am Chem Soc. 2004 Nov 17;126(45):14746-51
Authors: Etzkorn M, Böckmann A, Lange A, Baldus M
A general NMR strategy to directly study molecular interfaces under magic angle spinning is introduced. The approach is based on the spectroscopic analysis of uniformly, but heterogeneously, labeled molecular mixtures containing the spin species X and Y (X:Y). For the case of an ((15)N:(13)C) labeled sample, the use of NC, NHC, and NHHC transfers is demonstrated. Applied to the ((13)C:(15)N) labeled dimeric form of the 85 amino acid protein Crh, the NHHC approach reveals a variety of monomer-monomer interactions in the microcrystalline state.
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Biochim Biophys Acta. 2011 Aug 3;
Authors: Gustavsson M, Traaseth NJ, Veglia G
In this paper, we analyzed the ground and excited states of phospholamban (PLN), a membrane protein that regulates sarcoplasmic reticulum calcium ATPase (SERCA), in different membrane mimetic environments....
[NMR paper] Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Related Articles Solid-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...
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[NMR paper] Probing membrane protein orientation and structure using fast magic-angle-spinning so
Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.
Related Articles Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.
J Biomol NMR. 2004 Nov;30(3):253-65
Authors: Andronesi OC, Pfeifer JR, Al-Momani L, Ozdirekcan S, Rijkers DT, Angerstein B, Luca S, Koert U, Killian JA, Baldus M
One and two-dimensional solid-state NMR experiments are discussed that permit probing local structure and overall molecular conformation of membrane-embedded polypeptides...
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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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[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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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...
Probing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures wi
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