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Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints

  1. Author:
    Gaponenko, V.
    Sarma, S. P.
    Altieri, A. S.
    Horita, D. A.
    Li, J.
    Byrd, R. A.

  2. Author Address

    Byrd, RA, NCI, Struct Biophys Lab, POB B, Frederick, MD 21702 USA NCI, Struct Biophys Lab, Frederick, MD 21702 USA.
    1. Year: 2004
  2. Journal: Journal of Biomolecular Nmr
    1. 28
    2. 3
    3. Pages: 205-212
  4. Type of Article: Article
  1. Abstract:

    We demonstrate improved accuracy in protein structure determination for large (greater than or equal to 30 kDa), deuterated proteins (e.g. STAT4(NT)) via the combination of pseudocontact shifts for amide and methyl protons with the available NOEs in methyl-protonated proteins. The improved accuracy is cross validated by Q-factors determined from residual dipolar couplings measured as a result of magnetic susceptibility alignment. The paramagnet is introduced via binding to thiol-reactive EDTA, and multiple sites can be serially engineered to obtain data from alternative orientations of the paramagnetic anisotropic susceptibility tensor. The technique is advantageous for systems where the target protein has strong interactions with known alignment media

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