Nuclear magnetic resonance spectroscopy high-resolution spectra

Fig. 3.73 Decoupled spectrum of crotonaldehyde. Data reproduced from W. McFarlane and R. F. M. White (1972). Techniques of High Resolution Nuclear Magnetic Resonance Spectroscopy. London Butterworths, p. 28.

FIGURE 7-17 High resolution H spectrum of ethanol (redrawn from the data of L. M. Jackman and S. Stemhell, Nuclear Magnetic Resonance Spectroscopy in Organic Chemistry, Peigamon Press, 1969). 

Nuclear magnetic resonance spectroscopy is likely the most versatile method for the study of biomolecules. The power of NMR originates from the fact that practically every atom with a magnetic nucleus gives rise to an individual signal in the NMR spectrum that carries spatial and temporal information of the local chemical environment of that atom. Solution conditions in high resolution NMR experiments mimic the natural biological environment and results relate to functional assays. 

We present a solid-state nuclear magnetic resonance (NMR) experiment that allows the observation of a high-resolution two-dimensional heteronuclear correlation (2D HETCOR) spectrum between aluminum and phosphorous in aluminophosphate molecular sieve VPI-5. The experiment uses multiple quantum magic angle spinning (MQMAS) spectroscopy to remove the second order quadrupolar broadening in Al nuclei. The magnetization is then transferred to spin-1/2 nuclei of P via cross polarization (CP) to produce for the first time isotropic resolution in both dimensions. 

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