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Cavity formation before stable hydrogen bonding in the folding of a β-clam protein

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The time course of folding of a small β-sheet protein reveals formation of a central ligand binding cavity before the consolidation of the native hydrogen bonding network. These results suggest that side chain interactions and not stable hydrogen bonding determine the β-sheet architecture and play crucial roles in the overall chain topology.

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Author notes

  1. Patricia L. Clark

    Present address: Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

Authors and Affiliations

  1. Molecular Biophysics Graduate Program, University of Texas Southwestern Medical Center, Dallas, Texas, 75235, USA

    Patricia L. Clark

  2. Department of Molecular Biology and Oncology, University of Texas Southwestern Medical Center, Dallas, Texas, 75235, USA

    Zhi-Ping Liu

  3. Departments of Biochemistry and Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, 75235, USA

    Josep Rizo

  4. Department of Chemistry, University of Massachusetts, Amherst, Massachusetts, 01003, USA

    Lila M. Gierasch

Authors
  1. Patricia L. Clark
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  2. Zhi-Ping Liu
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  3. Josep Rizo
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  4. Lila M. Gierasch
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Clark, P., Liu, ZP., Rizo, J. et al. Cavity formation before stable hydrogen bonding in the folding of a β-clam protein. Nat Struct Mol Biol 4, 883–886 (1997). https://doi.org/10.1038/nsb1197-883

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