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Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes.

Wang S, Zhou P
J Biomol NMR 59 51-6 (2014)
Cited: 5 times
EuropePMC logo PMID: 24789524

Abstract

Unambiguous detection and assignment of intermolecular NOEs are essential for structure determination of protein complexes by NMR. Such information has traditionally been obtained with 3-D half-filtered experiments, where scalar coupling-based purging of intramolecular signals allows for selective detection of intermolecular NOEs. However, due to the large variation of (1)JHC scalar couplings and limited chemical shift dispersion in the indirect proton dimension, it is difficult to obtain reliable and complete assignments of interfacial NOEs. Here, we demonstrate a strategy that combines selective labeling and high-resolution 4-D NOE spectroscopy with sparse sampling for reliable identification and assignment of intermolecular NOEs. Spectral subtraction of component-labeled complexes from a uniformly-labeled protein complex yields an "omit" spectrum containing positive intermolecular NOEs with little signal degeneracy. Such a strategy can be broadly applied to unbiased detection, assignment and presentation of intermolecular NOEs of protein complexes.

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  1. Flagellum inheritance in Trypanosoma brucei requires a kinetoplastid-specific protein phosphatase. Zhou Q, Dong G, Li Z. J Biol Chem 293 8508-8520 (2018)
  2. Reduced Point Charge Models of Proteins: Effect of Protein-Water Interactions in Molecular Dynamics Simulations of Ubiquitin Systems. Leherte L, Vercauteren DP. J Phys Chem B 121 9771-9784 (2017)


Reviews citing this publication (1)

  1. Applications of high dimensionality experiments to biomolecular NMR. Nowakowski M, Saxena S, Stanek J, Żerko S, Koźmiński W. Prog Nucl Magn Reson Spectrosc 90-91 49-73 (2015)

Articles citing this publication (2)

  1. The experimental accuracy of the uni-directional exact NOE. Strotz D, Orts J, Minges M, Vögeli B. J Magn Reson 259 32-46 (2015)
  2. Ubiquitin recognition by FAAP20 expands the complex interface beyond the canonical UBZ domain. Wojtaszek JL, Wang S, Kim H, Wu Q, D'Andrea AD, Zhou P. Nucleic Acids Res 42 13997-14005 (2014)


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