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Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy

Authors

  • Dr. Pramodh Vallurupalli,

    Corresponding author
    1. Departments of Molecular Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario, M5S1A8 (Canada)
    • Departments of Molecular Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario, M5S1A8 (Canada)
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  • Prof. Lewis E. Kay

    Corresponding author
    1. Departments of Molecular Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario, M5S1A8 (Canada)
    2. Program in Molecular Structure and Function, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, M5G1X8 (Canada)
    • Departments of Molecular Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario, M5S1A8 (Canada)
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  • We would like to thank Dr. Guillaume Bouvignies for providing the ChemEX program used in data analysis and Dr. Eriks Kupce for valuable discussions. L.E.K. holds a Canada Research Chair in Biochemistry. The work was supported by grants from the CIHR and NSERC Canada.

Abstract

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Unsichtbares sichtbar machen: Ein 13CO-NMR-CEST-Experiment (CEST=chemical exchange saturation transfer) wurde zur Untersuchung „unsichtbarer“ angeregter Proteinzustände mit Lebensdauern von 5 bis 50 ms entwickelt. Die chemischen 13CO-Verschiebungen zusammen mit den 15N-CEST-Profilen zeigen, dass die A39G-FF-Domäne sich ähnlich wie das Wildtypprotein über ein kompaktes Intermediat (I) faltet (F und U=nativer bzw. ungefalteter Zustand).

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