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TROSY-Based Correlation and NOE Spectroscopy for NMR Structural Studies of Large Proteins

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Protein NMR Techniques

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 278))

Abstract

Transverse relaxation-optimized spectroscopy (TROSY) is based on the fact that cross-correlation relaxation rates associated with the interferences between chemical shift anisotropy and dipole-dipole interactions can be dramatically reduced. TROSY selects these slowly relaxing components of 15N–1HN or 13C–1H antiphase coherences to significantly enhanced signal sensitivity and spectral resolution for large proteins (>30 kD). The basic principles and applications of three- and four-dimensional TROSY-based triple-resonance experiments and NOESY experiments for structure-function studies of proteins are discussed in this chapter. To make applications of these experiments easier, some of the experimental setups are also described.

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Author information

Authors and Affiliations

  1. Department of Biochemistry, The Hong Kong University of Science and Technology, Hong Kong, SAR, People’s Republic of China

    Guang Zhu & Donghai Lin

  2. Department of Chemistry, University of Houston, TX

    Youlin Xia & Xiaolian Gao

Authors
  1. Guang Zhu
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  2. Youlin Xia
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  3. Donghai Lin
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  4. Xiaolian Gao
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Editor information

Editors and Affiliations

  1. Department of Biochemistry, University of Oxford, Oxford, UK

    A. Kristina Downing

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© 2004 Humana Press Inc., Totowa, NJ

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Zhu, G., Xia, Y., Lin, D., Gao, X. (2004). TROSY-Based Correlation and NOE Spectroscopy for NMR Structural Studies of Large Proteins. In: Downing, A.K. (eds) Protein NMR Techniques. Methods in Molecular Biology™, vol 278. Humana Press. https://doi.org/10.1385/1-59259-809-9:057

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  • DOI: https://doi.org/10.1385/1-59259-809-9:057

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-246-9

  • Online ISBN: 978-1-59259-809-0

  • eBook Packages: Springer Protocols

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