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Protein NMR spectroscopy in structural genomics

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Abstract

Protein NMR spectroscopy provides an important complement to X-ray crystallography for structural genomics, both for determining three-dimensional protein structures and in characterizing their biochemical and biophysical functions.

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Figure 1: Comparison of 15N-1H correlation spectra for disordered and well-folded proteins.
Figure 2: Distribution of predicted open reading frame (ORF) lengths in the genomes of Escherichia coli (blue), Saccharomyces cerevisiae (red), Caenorhabditis elegans (yellow), and Drosophila melanogaster (green).
Figure 3: Results of automatic analysis of protein structures from NMR data.

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Acknowledgements

We thank S. Anderson for useful discussions. The NMR data for FGF were provided by R. Powers and F. Moy (Wyeth Ayerst Research Laboratories). G.T.M. is supported by grants from the New Jersey Commission on Science and Technology, The National Science Foundation, and the Merck Genome Research Institute. K.C.G. is supported by Postdoctoral Fellowship Award from the NIH.

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Authors and Affiliations

  1. Department of Molecular Biology and Biochemistry, Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway , 08854-5638, New Jersey, USA

    Gaetano T. Montelione, Deyou Zheng, Yuanpeng J. Huang & Kristin C. Gunsalus

  2. Department of Chemistry, State University of New York at Buffalo, Buffalo, 14260, New York, USA

    Thomas Szyperski

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  1. Gaetano T. Montelione
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  2. Deyou Zheng
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Correspondence to Gaetano T. Montelione.

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Montelione, G., Zheng, D., Huang, Y. et al. Protein NMR spectroscopy in structural genomics. Nat Struct Mol Biol 7 (Suppl 11), 982–985 (2000). https://doi.org/10.1038/80768

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