The well-resolved 1H solid state NMR spectra of alanine tripeptide (Ala3) with anti-parallel and parallel � sheet structures are assigned by using double-quantum magic-angle-spinning (DQMAS) measurements with ultra high field and ultra fast MAS NMR. The observed 1H chemical shifts are in excellent agreement with the 1H chemical shifts calculated by first principles gauge-including projector augmented wave (GIPAW) method for 1H geometry optimized structures, indicating the accurate 1H positions of the structure. The chemical shifts of the amide protons are described by the inverse third power of inter-molecular NH�OC direct hydrogen bond distance. We applied this relationship to evaluate the inter-molecular hydrogen bond distances of silk structures, silk I and silk II.

Probing intermolecular structures of biomolecules in solid state: High resolution <sup>1</sup>H solid state NMR analysis under ultra high speed MAS

245th National Meeting (2013)

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Probing intermolecular structures of biomolecules in solid state: High resolution 1H solid state NMR analysis under ultra high speed MAS

Probing intermolecular structures of biomolecules in solid state: High resolution ¹H solid state NMR analysis under ultra high speed MAS