Nuclear magnetic resonance three-dimensional structure elucidation

A crucial question is. What does the three-dimensional structure of a specific protein look like Protein structure determines function, given that the specificity of active sites and binding sites depends on the precise threedimensional conformation. Nuclear magnetic resonance spectroscopy and x-ray crystallography are two of the most important techniques for elucidating the conformation of proteins. 

Structural studies, particularly those that elucidate the three-dimensional relationships of the amino acid residues in the enzyme, permit judgments about whether the involvement of one or the other side chain is physically and sterically possible. Such techniques include nuclear magnetic resonance, electron spin resonance, single-crystal x-ray diffraction, and cross-linking studies. The important question to be answered by mechanistic studies is how an enzyme catalyzes a particular reaction so rapidly. Two general factors seem to be involved. 

The analysis of lipids is dominated by chromatographic methods such as gas chromatography (GC) and high-pressure liquid chromatography (HPLC) and some other physical methods such as thermo analysis. Nuclear magnetic resonance (NMR) spectroscopy covers only a small part of lipid analysis. In most cases it is used for qualitative analysis such as structure elucidation of lipids. Unlike the other methods NMR spectroscopy is coupled with computer technology, and its development is as fast as that of computer software and hardware. In 1991 the Nobel Prize for chemistry was given to Professor Ernst for the development of Fourier Transform NMR spectroscopy (FT-NMR). The capabilities of these methods even for the elucidation of the three-dimensional structures of small molecules up to macromolecules are impressive. 

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