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Protein alchemy: Changing β-sheet into α-helix

Nature Structural Biology volume 4, pages 548–552 (1997)Cite this article

Abstract

For most proteins the amino acid sequence determines the tertiary structure. The relative importance of the individual amino acids in specifying the fold, however, remains unclear. To highlight this. Creamer and Rose put forth the ‘Paracelsus challenge’: Design a protein with 50% sequence identity to a protein with a different fold. We have met this challenge by designing a sequence which retains 50% identity to a predominantly β-sheet protein, but which now adopts a four helix bundle conformation and possesses the attributes of a native protein. Our results emphasize that a subset of the amino acid sequence is sufficient to specify a fold, and have implications both for structure prediction and design.

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Authors and Affiliations

  1. Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT, 06520, USA

    Suganthi Balasubramanian & Lynne Regan

  2. Department of Chemistry, Yale University, 266 Whitney Avenue, New Haven, CT, 06520, USA

    Seema Dalal

Authors
  1. Seema Dalal
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  2. Suganthi Balasubramanian
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  3. Lynne Regan
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Dalal, S., Balasubramanian, S. & Regan, L. Protein alchemy: Changing β-sheet into α-helix. Nat Struct Mol Biol 4, 548–552 (1997). https://doi.org/10.1038/nsb0797-548

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  • DOI: https://doi.org/10.1038/nsb0797-548

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