NMR and Structure Determination

The spectral assignment process, complex as it is, is only a prelude to the use of NMR data to assist in the final determination of the three-dimensional structure of the protein. Here, the most important experiment is NOESY, often in conjunction with HMQC or other methods for spreading out the 2D NOESY peaks in three or four dimensions. For larger proteins 4D experiments are essential to spread the NOESY peaks according to both 13C and 15N chemical shifts. We 

FIGURE 13.10 Illustration of correlations found in a number of different experiments for the protein calmodulin. From Ikura et al123 

This distance information is augmented with data on the conformation of sections of the polypeptide chain, obtained from a suitably parameterized Karplus 

FIGUR 13.11 Illustration of the three-dimensional structure of the protein cyanovirin-N, as determined by NMR methods. From Bewley et al,124 

Application of NMR to three-dimensional structure determination is covered in several books, including NMR of Proteins and Nucleic Acids by Kurt Wiithrich,60 NMR of Proteins edited by G. M. Clore and A. M. Gronenborn,131 Biomolecular NMR Spectroscopy by Jeremy Evans,132 and Protein NMR Spectroscopy by John Cavanagh et al,120 

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Meadows RP, Nikonowicz EP, Jones CR, BastianJW, and Goresterin DG. Two Dimensional NMR and Structure Determination of Salmon Calcitonin in Methanol. Biochemistry 1991 30 1245-1247. 

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