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Efficient and precise measurement of H-alpha-C-alpha, C-alpha-C ', C-alpha-C-beta and H-N-N residual dipolar couplings from 2D H-N-N correlation spectra

  1. Author:
    McFeeters, R.
    Fowler, C.
    Gaponenko, V.
    Byrd, R.

  2. Author Address

    NCI, Macromol NMR Sect, Struct Biophys Lab, Frederick, MD 21702 USA Byrd, R, NCI, Macromol NMR Sect, Struct Biophys Lab, Frederick, MD 21702 USA
    1. Year: 2005
    2. Date: JAN
  2. Journal: Journal of Biomolecular Nmr
    1. 31
    2. 1
    3. Pages: 35-47
  4. Type of Article: Article
  1. Abstract:

    A suite of experiments are presented for the measurement of H-alpha-C-alpha, C-alpha-C', C-alpha-C-beta and H-N-N couplings from uniformly N-15, C-13 labeled proteins. Couplings are obtained from a series of intensity modulated two-dimensional H-N-N spectra equivalent to the common H-1-N-15-HSQC spectra, alleviating many overlap and assignment issues associated with other techniques. To illustrate the efficiency of this method, H-alpha-C-alpha, C-alpha-C', and H-N-N isotropic scalar couplings were determined for ubiquitin from data collected in less than 4.5 h, C-alpha-C-beta data collection required 10 h. The resulting couplings were measured with an average error of +/-0.06, +/-0.05, +/-0.04 and +/-0.10 Hz, respectively. This study also shows H-alpha-C-alpha and C-alpha-C-beta couplings, valuable because they provide orientation of bond vectors outside the peptide plane, can be measured in a uniform and precise way. Superior accuracy and precision to existing 3D measurements for C-alpha-C' couplings and increased precision compared to IPAP measurements for H-N-N couplings are demonstrated. Minor modi. cations allow for acquisition of modulated H-N-C' 2D spectra, which can yield additional well resolved peaks and significantly increase the number of measured RDCs for proteins with crowded H-1-N-15 resonances

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  1. View record in Web of Science®
  2. WOS: 000226940200004

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