Nuclear magnetic resonance spectroscopy advantages

Elipe, M.V.S., Advantages and disadvantages of nuclear magnetic resonance spectroscopy as a hyphenated technique, Anal. Chim. Acta., 497, 1-25 (2003). 

Most of our structural information comes from x-ray crystallographic analysis of protein crystals and from the use of nuclear magnetic resonance spectroscopy in solution. Each of these techniques has advantages and limitations which makes them suitable for a complementary range of problems. The first protein structure determined at a sufficient resolution to trace the path of the polypeptide chain was that of myoglobin in 1960. Since that time many thousands of structures corresponding to hundreds of different proteins have been determined. The coordinates of the atoms in many protein and nucleic acid structures are available from the Protein Data Bank, which may be accessed via the Internet or World Wide Web (http //www.pdb.bnl.gov). 

The molecular beam subsequently played a central role in the invention of nuclear magnetic resonance spectroscopy (see Tools of the Trade, Chapter 5) and formed the experimental basis for Nobel Prize-winning studies of chemical reactions. It has become a routine tool in many other forms of spectroscopy and is used in industry for molecular beam epitaxy, which takes advantage of the technology to grow carefully tailored semiconductor crystals. 

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