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Automation of NMR structure determination of proteins

  1. Author:
    Altieri, A. S.
    Byrd, R. A.

  2. Author Address

    NCI, Canc Res Ctr, Struct Biophys Lab, Frederick, MD 21702 USA Altieri, AS, NCI, Canc Res Ctr, Struct Biophys Lab, Frederick, MD 21702 USA
    1. Year: 2004
    2. Date: OCT
  2. Journal: Current Opinion in Structural Biology
    1. 14
    2. 5
    3. Pages: 547-553
  4. Type of Article: Review
  1. Abstract:

    The automation of protein structure determination using NMR is coming of age. The tedious processes of resonance assignment, followed by assignment of NOE (nuclear Overhauser enhancement) interactions (now intertwined with structure calculation), assembly of input files for structure calculation, intermediate analyses of incorrect assignments and bad input data, and finally structure validation are all being automated with sophisticated software tools. The robustness of the different approaches continues to deal with problems of completeness and uniqueness; nevertheless, the future is very bright for automation of NMR structure generation to approach the levels found in X-ray crystallography. Currently, near completely automated structure determination is possible for small proteins, and the prospect for medium-sized and large proteins is good

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  2. DOI: 10.1016/j.sbi.2004.09.003
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