Evaluation of current techniques for Ab initio protein structure prediction

Authors

  • Tom Defay,

    1. Graduate Group in Biophysics, University of California, San Francisco, California 94131-0450
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  • Dr. Fred E. Cohen

    Corresponding author
    1. Departments of Pharmaceutical Chemistry, Biochemistry and Biophysics, Medicine, and Cellular and Molecular Pharmacology, University of California, San Francisco, California 94131-0450
    • Department of Cellular and Molecular Pharmacology, University of California, San Francisco, 513 Parnassus Ave., San Francisco, CA 94131-0450
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Abstract

The results of a protein structure prediction contest are reviewed. Twelve different groups entered predictions on 14 proteins of known sequence whose structures had been determined but not yet disseminated to the scientific community. Thus, these represent true tests of the current state of structure prediction methodologies. From this work, it is clear that accurate tertiary structure prediction is not yet possible. However, protein fold and motif prediction are possible when the motif is recognizably similar to another known structure. Internal symmetry and the information inherent in an aligned family of homologous sequences facilitate predictive efforts. Novel folds remain a major challenge for prediction efforts. © 1995 Wiley-Liss, Inc.

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