N–H Spin–Spin Couplings: Probing Hydrogen Bonds in Proteins

Authors

  • Sheng-Qi Xiang,

    1. Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen (Germany)
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  • Raghavendran L. Narayanan,

    1. Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen (Germany)
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  • Dr. Stefan Becker,

    1. Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen (Germany)
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  • Prof. Markus Zweckstetter

    Corresponding author
    1. Max-Planck-Institut für Biophysikalische Chemie & Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Am Fassberg 11, 37077 Göttingen (Germany)
    • Max-Planck-Institut für Biophysikalische Chemie & Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Am Fassberg 11, 37077 Göttingen (Germany)
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  • We thank Dr. Jacek Biernat and Dr. Eckhard Mandelkow for providing Tau samples.

Abstract

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Sensitive information: Hydrogen bonds stabilize protein structures and are critical for many chemical and biological phenomena. NMR studies found that the one-bond 1H–15N scalar coupling constant is increased by up to 1.6 Hz when a hydrogen bond is formed. These coupling constants therefore provide a sensitive tool for studying protein structure.

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