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Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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De Novo-Designed β-Sheet Heme Proteins.

Areetha D'Souza1, Surajit Bhattacharjya1

  • 1School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.

Biochemistry
|February 3, 2021
PubMed
Summary

Researchers successfully designed functional beta-sheet peptides and miniproteins that bind heme. These novel proteins exhibit peroxidase activity and electron transfer capabilities in various environments, advancing de novo protein design.

Area of Science:

  • Biochemistry
  • Protein Engineering
  • Synthetic Biology

Background:

  • Heme is a crucial cofactor for protein function, often found in alpha-helical structures.
  • Designing beta-sheet proteins that bind heme is challenging due to aggregation tendencies.
  • Previous efforts focused on alpha-helical heme proteins, leaving beta-sheet designs less explored.

Purpose of the Study:

  • To review the successful design of novel multistranded beta-sheet heme-binding peptides.
  • To demonstrate the development of well-folded beta-sheet proteins in aqueous and membrane environments.
  • To highlight progress in creating functional beta-sheet proteins for diverse applications.

Main Methods:

  • De novo design of beta-hairpin peptides that self-assemble.

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  • Optimization of beta-hairpin structures for heme binding pockets within multistranded beta-sheets.
  • Characterization of soluble beta-sheet peptides and miniproteins for heme binding affinity and stability.

    • Main Results:

    • Designed beta-hairpin peptides self-assemble to bind heme and exhibit peroxidase activity in membranes.
    • Optimized beta-sheet structures accommodate heme for catalysis and electron transfer in membranes.
    • Developed soluble beta-sheet peptides and miniproteins with high affinity and stability for single and multiple heme binding.

    Conclusions:

    • Significant progress has been made in the de novo design of functional beta-sheet heme-binding proteins.
    • These designed beta-sheet proteins offer new possibilities for applications in catalysis and electron transfer.
    • The findings pave the way for broader exploration of beta-sheet scaffolds in protein engineering.