NMR spectroscopy of biological solids

NMR spectroscopy of biological solids

Ayyalusamy Ramamoorthy (ed)

Abingdon, UK: Taylor & Francis | 2005 | 400 pp | ?79.99 (HB) | ISBN 1574444964 

Reviewed by Jacek Klinowski 

The discovery in 1959 of magic-angle-spinning (MAS) by Raymond Andrew and colleagues at the University of North Wales, Bangor, UK, and by Irving Lowe at Washington University, St Louis, US, ushered in a new era in the structural study of solids.  

This very sensitive new probe for studying molecular structure enabled us to acquire high-resolution nuclear magnetic resonance (NMR) spectra of a wide range of materials of interest to chemistry, physics, biology, and materials and earth sciences. However, because of technical difficulties, it is only within the past 20 years that the full potential of the method has been exploited.  

Unlike x-ray diffraction, the other principal method of studying solids, NMR has the advantage that it can examine non-crystalline materials. In combination with other techniques, which involve a variety of complex and ingenious radiofrequency pulse sequences, MAS NMR can now be applied to a wide range of problems in many scientific fields. 

Biological solids do not yield easily to structural examination by chemists, who have difficulties in dealing with very large molecules. The chemical shifts of the thousands (or sometimes hundreds of thousands) of component atoms differ very little, and the dipolar interactions between the omnipresent protons broaden the NMR lines. In addition, experimentalists often have very small amounts of the (usually amorphous) sample at their disposal. It is therefore fascinating to see that these obstacles are being overcome. NMR is now providing invaluable information not only about new drugs, the study of which has become routine, but also about real ’life molecules’. 

This book, edited by Ayyalusamy Ramamoorthy, of the University of Michigan at Ann Arbor, US, focuses on the most important families of biological solids: proteins, peptides, lipid bilayers and nucleic acids. There are chapters on interatomic distance determination, spectral assignment, torsion angle determination, double-quantum resonance, sensitivity enhancement, computational aspects and the role of inorganic cations in nucleic acid chemistry. 

I was impressed to see that NMR can provide unprecedented insights into a field as fraught with difficulties as protein folding. While I would like to see an introductory chapter summarising the state of the art and identifying future areas of research, I consider this to be a valuable, useful and nicely produced book, of interest to all workers in the field.