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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.
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
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Enzyme stabilization via computationally guided protein stapling.

Eric J Moore1, Dmitri Zorine2,3, William A Hansen2,3,4

  • 1Department of Chemistry, University of Rochester, Rochester, NY 14627.

Proceedings of the National Academy of Sciences of the United States of America
|November 8, 2017
PubMed
Summary
This summary is machine-generated.

Enzyme stabilization is crucial for applications. A new computational method uses covalent staples to rapidly enhance enzyme stability and performance without compromising function.

Keywords:
Rosetta macromolecular modelingcomputational protein designmyoglobinnoncanonical amino acidsprotein thermostabilization

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Area of Science:

  • Biocatalysis and protein engineering
  • Computational protein design
  • Enzyme stabilization

Background:

  • Enzyme thermostabilization is essential for industrial applications.
  • Directed evolution is laborious and can reduce catalytic efficiency.
  • Need for efficient and non-disruptive protein stabilization methods.

Purpose of the Study:

  • To develop a minimally invasive strategy for enzyme stabilization using computational design.
  • To create robust myoglobin-based cyclopropanation biocatalysts.
  • To enhance enzyme stability without sacrificing catalytic function.

Main Methods:

  • Genetically encoding nonreducible covalent staples into protein scaffolds.
  • Utilizing computational design for targeted staple installation.
  • Assessing thermostability (Tm, T50) and chemical denaturation (Cm) changes.

Main Results:

  • Achieved significant thermostability increases (ΔTm = +18.0 °C, ΔT50 = +16.0 °C).
  • Enhanced stability against chemical denaturation (ΔCm = +0.53 M GndHCl).
  • Maintained catalytic efficiency and stereoselectivity; improved performance in organic cosolvents.

Conclusions:

  • Introduced a rapid, computationally designed covalent stapling approach for protein stabilization.
  • Demonstrated enhanced stability and performance of myoglobin biocatalysts.
  • Validated a broadly applicable method for protein and enzyme engineering.