Peptides solid state hydrogen bonding/ordering

In addition to the use of H, C, and N NMR chemical shifts, it has been shown that observation of solid-state chemical shifts and quadrupolar couplings adds important information on the higher-ordered and hydrogen-bonded structures of polypeptides and peptides in the solid state [62-65], Solid-state NMR has been shown to be useful, moreover, for determining the local structures of alkali silicates [66-70]. Therefore, it is expected that solid-state NMR may reveal further dimensions of the structural and dynamic behavior of PDES in the crystalline, biphasic, and isotropic phases, in addition to the H, C, and Si NMR results reported previously. Due to the low natural abundance of nuclei (0.037%), the NMR analysis requires labeling. The structure and dynamics of 0-enriched... 

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