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Transverse Relaxation Optimized Spectroscopy

  • Chapter
Protein NMR for the Millennium

Part of the book series: Biological Magnetic Resonance ((BIMR,volume 20))

Abstract

TROSY represents a spectroscopic contribution in a constant pursuit of NMR structures of ever larger proteins, nucleic acids and their complexes. As it was theoretically predicted and proven in practice the most efficient application of TROSY is achieved in combination with the selective or uniform deuteration of biomolecules, in particular proteins. In this way biomolecular particles with the molecular sizes exceeding 100 kDa have now become amenable for high resolution NMR studies. Due to its simplicity and flexibility the TROSY principle has also been integrated into many other NMR applications not necessary targeting extremely large biomolecues. TROSY-based NMR experiments have been developed for the detection and characterization of weak interactions such as scalar couplings across hydrogen bonds and residual dipolar couplings. The use of TROSY in Nuclear Overhauser spectroscopy might significantly facilitate the spectral analysis by suppressing the strong diagonal peaks benefiting studies of a wide range of biomolecules.

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Authors and Affiliations

  1. Laboratorium für Physikalische Chemie, Eidgenössische Technische Hochschule, CH-8092, Zürich, Switzerland

    Konstantin V. Pervushin

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Editors and Affiliations

  1. University of Alabama at Birmingham, Birmingham, Alabama

    N. Rama Krishna

  2. University of Denver, Denver, Colorado

    Lawrence J. Berliner

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Pervushin, K.V. (2002). Transverse Relaxation Optimized Spectroscopy. In: Krishna, N.R., Berliner, L.J. (eds) Protein NMR for the Millennium. Biological Magnetic Resonance, vol 20. Springer, Boston, MA. https://doi.org/10.1007/0-306-47936-2_1

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