Spectroscopy solid-state nuclear magnetic resonance

Solid-state nuclear magnetic resonance spectroscopy (SSNMR) [13]... 

Hoh, K.P., Ishida, H. and Koenig, J.L. (1990). Silicon-29 solid state nuclear magnetic resonance spectroscopy of composite interfaces. Polym. Composites 11, 121 125. 

Kinetic gelation models [178] have been used to determine, within experimental error, the fraction of constrained and unconstrained double bonds over a wide range of conversions in the polymerization of ethylene glycol dimethacrylate. The amount of unconstrained and constrained functional groups was determined experimentally by solid state nuclear magnetic resonance spectroscopy. The rules for determining constraint in the model were that all pendant double bonds and all monomers in pools of six or less are constrained. Monomers in pools of seven or more are assumed to be unconstrained. Whether a site is constrained or not does not affect the reactivity only the analysis of the model is affected by the rules defining constraint. 

SOLID STATE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY (MAS NMR)... 

Byrn SE, Bugay DE, Tishmack PA. Solid state nuclear magnetic resonance spectroscopy—pharmaceutical applications. J Pharm Sci 2003 92(3) 441-474. 

Wheat starch lysophospholipid forms tiny liposomes in water that could readily be transported into the interior of a starch granule during its development. Solid-state nuclear magnetic resonance spectroscopy suggests that the phospholipids in wheat starch are predominantly complexed with amylose in an amorphous form in the granules.354-356... 

Solid state nuclear magnetic resonance spectroscopy... 

Solid state nuclear magnetic resonance spectroscopy provides information on the environment of individual atoms. In essence, the change in environment of any atom can arise from two factors, which usually are not separable in the interpretation of the SSNMR spectra, but are conceptually independent. Since different polymorphs are different crystal structures, it is expected that the crystal environment of at least some atoms will differ from polymorph to polymorph (Section 2.4.2). In addition, since the molecular conformation may also vary among polymorphs (Section 5.6), the change in the environment of an atom due to conformational differences will also be reflected in the SSNMR (Levy et al. 1980 Bugay 2001 Strohmeier et al. 2001). 

Bugay, D. E. (1993). Solid-state nuclear magnetic resonance spectroscopy theory and pharmaceutical applications. Pharm. Res., 10, 317-27. [134f, 142]... 

Fletton, R. A., Lancaster, R. W., Harris, R. K., Kenwright, A. M., Packer, K. J., Waters, D. N. and Yeadon, A. (1986). A comparative spectroscopic investigation of two polymorphs of 4 -methyl-2 -nitroacetanilide using solid-state infrared and high-resolution solid-state nuclear magnetic resonance spectroscopy. J. Chem. Soc. Perkin Trans. 2,1705-9. [224]... 

Harris, R. K. (1985). Quantitative aspects of high-resolution solid-state nuclear magnetic resonance spectroscopy. The Analyst, 110, 649-55. [142]... 

Wilson M. A. (1989) Solid-state nuclear magnetic resonance spectroscopy of humic substances basic concepts and techniques. In Humic Substances II in Search of Structure (eds. M. H. B. Hayes, P. MacCarthy, R. L. Malcolm, and M. J. Swift). Wiley, pp. 309-338. 

Moisture was known to increase the mobility of the surface groups of protein as measured by solid-state nuclear magnetic resonance spectroscopy The distribution of water between the protein and the excipients in a freeze-dried powder depends on the crystalline or amorphous nature of the excipients. For example, if a protein is formulated with an amorphous excipient and stored in a sealed container, water would distribute according to the water affinity of the protein and excipients.When the amorphous excipient crystallizes (e.g., because of elevated temperatures), it will expel its sorbed water, which may cause stability problems in the protein. ... 

Bugay, D.E. Solid-state nuclear magnetic resonance spectroscopy. Drugs Pharm. Sci. 2002,117,467-499. Handbook of Pharmaceutical Analysis. 

Bechinger, B., Zasloff, M. and Opella, S. J. (1998) Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy. Biophysical Journal, 74, 981-987. 

Helmus JJ, Surewicz K, Surewicz WK, Jaroniec CP (2010) Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy. J Am Chem Soc 132 2393-2403... 

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