Nuclear magnetic resonance examples

Lauterbur P C 1973 Image formation by induced local interactions examples employing nuclear magnetic resonance Nature 242 190-1... 

These two references give an excellent overview over the most recent examples in this research field. Callaghan P T 1993 Principles of Nuclear Magnetic Resonance Microscopy (Oxford Clarendon)... 

No molecule is completely rigid and fixed. Molecules vibrate, parts of a molecule may rotate internally, weak bonds break and re-fonn. Nuclear magnetic resonance spectroscopy (NMR) is particularly well suited to observe an important class of these motions and rearrangements. An example is tire restricted rotation about bonds, which can cause dramatic effects in the NMR spectrum (figure B2.4.1). 

Nuclear magnetic resonance (nmr) is a nondestmctive means of measuring the amount of hydrogen in various materials for example, nmr has been used to determine the hydrogen content of coals (251). 

In the following, some examples of applications of Fourier transform infrared (FTIR) Spectroscopy and of solid-state nuclear magnetic resonance (NMR) to the study of polymorphism in polymers are described. 

See, for example, Emsley JW (ed) (1985) Nuclear magnetic resonance in liquid crystals. Reidel, Dordrecht... 

P. T. Callaghan 1994, Principles of Nuclear Magnetic Resonance Microscopy, Clarendon Press, Oxford, 490 pp. Standard reference textbook for imaging, some examples but with a focus on theory. 

To obtain statistically significant comparisons of ordered and disordered sequences, much larger datasets were needed. To this end, disordered regions of proteins or wholly disordered proteins were identified by literature searches to find examples with structural characterizations that employed one or more of the following methods (1) X-ray crystallography, where absence of coordinates indicates a region of disorder (2) nuclear magnetic resonance (NMR), where several different features of the NMR spectra have been used to identify disorder and (3) circular dichroism (CD) spectroscopy, where whole-protein disorder is identified by a random coil-type CD spectrum. 

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