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Automated solid-state NMR resonance assignment of protein microcrystals and amyloids

Schmidt, Elena ; Gath, Julia ; Habenstein, Birgit ; Ravotti, Francesco ; Székely, Kathrin ; Huber, Matthias ; Buchner, Lena ; Böckmann, Anja ; Meier, Beat ; Güntert, Peter

In: Journal of Biomolecular NMR, 2013, vol. 56, no. 3, p. 243-254

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    Titre
    • Automated solid-state NMR resonance assignment of protein microcrystals and amyloids
    Auteur
    • Schmidt, Elena. Center for Biomolecular Magnetic Resonance, Institute of Biophysical Chemistry, Goethe University Frankfurt am Main, Frankfurt am Main, Germany
    • Gath, Julia. Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    • Habenstein, Birgit. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Ravotti, Francesco. Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    • Székely, Kathrin. Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    • Huber, Matthias. Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    • Buchner, Lena. Center for Biomolecular Magnetic Resonance, Institute of Biophysical Chemistry, Goethe University Frankfurt am Main, Frankfurt am Main, Germany
    • Böckmann, Anja. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Meier, Beat. Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    • Güntert, Peter. Center for Biomolecular Magnetic Resonance, Institute of Biophysical Chemistry, Goethe University Frankfurt am Main, Frankfurt am Main, Germany
    Type de document
    • Postprint
    Langue
    • Inglese
    Publié dans
    • Journal of Biomolecular NMR, 2013, vol. 56, no. 3, p. 243-254. Springer Netherlands
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:312806
    Summary
    Solid-state NMR is an emerging structure determination technique for crystalline and non-crystalline protein assemblies, e.g., amyloids. Resonance assignment constitutes the first and often very time-consuming step to a structure. We present ssFLYA, a generally applicable algorithm for automatic assignment of protein solid-state NMR spectra. Application to microcrystals of ubiquitin and the Ure2 prion C-terminal domain, as well as amyloids of HET-s(218-289) and α-synuclein yielded 88-97% correctness for the backbone and side-chain assignments that are classified as self-consistent by the algorithm, and 77-90% correctness if also assignments classified as tentative by the algorithm are included