Abstract
Solid-state 17O NMR spectra of glycine-residue containing polypeptides in the solid state were successfully measured by using high-speed magic-angle-spinning (MAS) at 25 kHz under 18.8 T magnetic field (800 MHz for 1H). Three kinds of NMR parameters, such as chemical shift ( δ), quadrupolar coupling constant ( e 2 qQ/ h) and asymmetric parameter ( η), were determined from the observed spectra by computer simulation. The relationship between the hydrogen bond length of the polypeptides and the determined NMR parameters was discussed.
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