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Material characterization methods chemical shift

Solid-state nuclear magnetic resonance (SSNMR) spectroscopy is a more advanced method for differentiating the polymorphs of a material. The substance is placed in a strong magnetic field and subjected to radiofrequency radiation. The individual nuclei experience different magnetic environments and thus show different changes in resonant frequency characterized by chemical shift. SSNMR spectra show sharp resonance at chemical shifts characteristic of the molecular and crystal structure. The polymorphs are differentiated by their characteristic spectra. [Pg.99]

X-ray photoelectron spectroscopy of atomic core levels (XPS or ESCA) is a very powerful tool for characterization of the chemical surrounding of atoms in molecules. In particular, since the method is very surface sensitive, it is possible to monitor the first stages of the interface formation, i.e., in our case the interaction between individual metal atoms and the polymer. Standard core level bonding energies are well known for common materials. However, in our case, we are studying new combinations of atoms and new types of structures for which there are no reference data available. In order to interpret the experimental chemical shifts it is useful to compare with theoretical estimates of the shifts. [Pg.29]

On-flow HPLC-NMR analysis can also be performed when sufficient material is available. It involves collecting the NMR data continuously as the sample passes through the probe. This is the most efficient method for stmcture evaluation by HPLC-NMR. The NMR data are represented in a 2-D plot where the x direction contains chemical shift information and they direction is representative of the LC retention time. The individual spectra can be extracted from the ID slices along the x axis if so desired. The resolutions in the individual spectra are of somewhat lower quality than in the stop-flow method however, the introduction of the second dimension allows for easy stmcture assignment even for overlapping peaks in the LC separation. As seen in Fig. 19, the on-flow HPLC-NMR characterization shows four distinct sets of resonances. [Pg.97]

Clarifying the structure and functions of protein materials in the solid state provides an index with respect to the design of artificial biomaterials. Solid-state NMR has been used as a powerful means for elucidating structure and dynamics in addition to the X-ray diffraction method [le]. The structure and dynamics of some fibrous proteins, such as wool, silk, collagen, tropomyosin, etc., have been characterized using characteristic solid-state NMR chemical shifts as stated above, and much more new information obtained in addition to the results provided by X-ray diffraction. And the individual advantages of these two methods are complementary with each other. Details of appli-... [Pg.831]


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