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  • Title: Rapidly-frozen polypeptide samples for characterization of high definition dynamics by solid-state NMR spectroscopy.
    Author: Lazo ND, Hu W, Lee KC, Cross TA.
    Journal: Biochem Biophys Res Commun; 1993 Dec 15; 197(2):904-9. PubMed ID: 7505577.
    Abstract:
    A method is described for defining anisotropic local dynamics in polypeptides by solid-state NMR. To avoid conformational heterogeneity introduced by large hexagonal ice crystals in low temperature hydrated samples, a fast-freezing technique is used for sample preparation. For a demonstration of this approach, the backbone librational motions of the gramicidin A channel conformation are studied in hydrated DMPC bilayers. The static 15N chemical shift tensor is characterized at 123 K for the Ala3 site. The temperature dependence of this tensor yields a determination of the librational amplitude and anisotropy of the motionally sampled space. This amplitude represents the sum of nanosecond and picosecond time-frame motions, both of which have a significant amplitude.
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