NMR Spectroscopic Detection of Protein Protons and Longitudinal Relaxation Rates between 0.01 and 50 MHz

Authors

  • Ivano Bertini Prof.,

    1. Magnetic Resonance Center and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271
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  • Yogesh K. Gupta,

    1. Magnetic Resonance Center and Department of Agricultural Biotechnology, University of Florence, P. le delle Cascine 28, 50144 Florence, Italy
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  • Claudio Luchinat Prof.,

    1. Magnetic Resonance Center and Department of Agricultural Biotechnology, University of Florence, P. le delle Cascine 28, 50144 Florence, Italy
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  • Giacomo Parigi Dr.,

    1. Magnetic Resonance Center and Department of Agricultural Biotechnology, University of Florence, P. le delle Cascine 28, 50144 Florence, Italy
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  • Christian Schlörb,

    1. Center for Biomolecular Magnetic Resonance and Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe University Frankfurt, Marie-Curie-Strasse 11, 60439 Frankfurt, Germany
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  • Harald Schwalbe Prof.

    1. Center for Biomolecular Magnetic Resonance and Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe University Frankfurt, Marie-Curie-Strasse 11, 60439 Frankfurt, Germany
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  • This work was supported by the European Union (contract HPRI-CT-2001-50028), by MIUR-FIRB, and by Ente Cassa di Risparmio di Firenze.

Abstract

original image

Relaxationszeit: Durch NMR-Spektroskopie bei 0.01–50 MHz wurden Dispersionsprofile der 1H-Relaxation in D2O bei millimolaren Konzentrationen erzeugt (siehe Bild). Die Untersuchung von Lysozym bei pH 3.5 (monomer) und pH 9.0 (dimer) sowie von α-Synuclein (entfaltet) lieferte direkte Informationen über die Aggregation anhand von Schätzungen der Korrelationszeit für die Umordnung und über die Kompaktheit des Proteins.

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