Proteins NMR spectroscopy

Cavanagh, J., Fairbrother, W.J., Palmer III, A.G., Skelton, N.J., and Ranee, M. 2006. Protein NMR Spectroscopy Principles and Practice, 2nd edition. Academic Press. 

A major limitation in using protein NMR spectroscopy in drug discovery has been the molecular weight limitation imposed by nuclear spin relaxation (line broadening) and increased spectral complexity associated with macromolecules larger than 35 kDa [5]. The most recent developments in NMR spectroscopy aimed at overcoming these problems will be briefly reviewed in Sect. 21.2. 

J. Cavanagh, W. J. Fairbrother, A. G. Palmer III, N.J. Skelton, Protein NMR Spectroscopy, Principles and Practice, Academic Press, 1996. 

Cavanagh J, Fairbrother WJ, Palmer AG 111, Skelton NJ (1996) Protein NMR Spectroscopy. Academic Press, San Diego, p 265... 

Traditional protein NMR spectroscopy of smaller proteins relies of 15N-filtered experiments, due to the relatively low expense of introducing 15N labels into proteins (compared to 13C) and the concomitant ability to use heteronuclear filtering to improve resolution in the H NMR dimension. Jelinek et al. were the first to demonstrate the ability to transfer this approach to peptides on TantaGel.80 They also showed the ability to detect pronounced peptide structure through the appearance of strong NOE correlations in 3H NOESY HRMAS spectra as shown in Fig. 8. This had important implications for the search of biological activity in peptides attached to supports, as the structure on the support may be different or more pronounced than in solution, if present at all in solution in peptides of this small size. 

P R E CONTENTS Preface. Stable-Isotope Assisted Protein NMR Spectroscopy in Solution, Brian J. Stockman and John L. Mar-kley. 31P and 1H Two-Dimensional NMR and NOESY-Dis-tance Restrained Molecular Dynamics Methodologies for Defining Sequence-Specific Variations in Duplex Oligonucleotides, David G. Gorenstein, Robert P. Meadows, James T. Metz, Edward Nikonowcz and Carol Beth Post. NMR Study of B- and Z-DNA Hairpins of d[(CG) 3T4(CG)3] in Solution, Sa-toshi Ikuta and Yu-Sen Wang. Molecular Dynamics Simulations of Carbohydrate Molecules, J.W. Brady. Diversity in the Structure of Hemes, Russell Timkovich and Laureano L. Bon-doc. Index. Volume 2,1991, 180 pp. 112.50/E72.50 ISBN 1-55938-396-8... 

Question What are the advantages and limitations of protein NMR spectroscopy ... 

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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