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Cooperative folding units of Escherichia coli tryptophan repressor

  1. Author:
    Wallqvist, A.
    Lavoie, T. A.
    Chanatry, J. A.
    Covell, D. G.
    Carey, J.

  2. Author Address

    Carey J Princeton Univ, Dept Chem Princeton, NJ 08544 USA Princeton Univ, Dept Chem Princeton, NJ 08544 USA NCI, Frederick Canc Res & Dev Ctr, Space Applicat Int Corp Frederick, MD 21702 USA
    1. Year: 1999
  2. Journal: Biophysical Journal
    1. 77
    2. 3
    3. Pages: 1619-1626
  4. Type of Article: Article
  1. Abstract:

    A previously published computational procedure was used to identify cooperative folding units within tryptophan repressor. The theoretical results predict the existence of distinct stable substructures in the protein chain for the monomer and the dimer. The predictions were compared with experimental data on structure and folding of the repressor and its proteolytic fragments and show excellent agreement for the dimeric form of the protein. The results suggest that the monomer, the structure of which is currently unknown, is likely to have a structure different from the one it has within the context of the highly intertwined dimer. Application of this method to the repressor monomer represents an extension of the computations into the realm of evaluating hypothetical structures such as those produced by threading. [References: 57]

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