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Non-classical Non-covalent σ-Hole Interactions in Protein Structure and Function: Concepts for Potential Protein

Margaret G Walker1, C Gustavo Mendez1, P Shing Ho1

  • 1Department of Biochemistry & Molecular Biology, 1870 Campus Delivery, Colorado State University, Fort Collins, CO, 80523-1870, USA.

Chemistry, an Asian Journal
|February 10, 2023
PubMed
Summary
This summary is machine-generated.

Nonclassical noncovalent interactions, including halogen, chalcogen, and tetrel bonds, significantly influence protein structure and function. These interactions, comparable in strength to hydrogen bonds, offer new avenues for designing functional proteins.

Keywords:
Noncovalent interactionschalcogen bondhalogen bondpeptidesprotein modificationstetrel bond

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Structural Biology

Background:

  • Biological molecule structure and function rely on noncovalent interactions, historically dominated by hydrogen bonds (H-bonds).
  • The σ-hole concept revealed diverse nonclassical noncovalent (ncNC) interactions beyond H-bonds, expanding applications in chemistry and biochemistry.
  • Halogen, chalcogen, and tetrel bonds are key ncNC interactions with significant electrostatic potential.

Purpose of the Study:

  • To review the impact of halogen, chalcogen, and tetrel bonds on peptide and protein structure, assembly, and function.
  • To highlight how these ncNC interactions can guide the design of novel functional proteins.
  • To explore the potential of synergistic ncNC interactions, such as H-bond enhanced X-bonds, in protein engineering.

Main Methods:

  • Review of existing literature on ncNC interactions in biological systems.
  • Analysis of natural and synthetic examples of halogen, chalcogen, and tetrel bonds in peptides and proteins.
  • Focus on studies demonstrating principles of stability, assembly, and catalysis mediated by these interactions.

Main Results:

  • Halogen, chalcogen, and tetrel bonds are integral to protein structure and function, comparable in energy to H-bonds.
  • These ncNC interactions play crucial roles in molecular recognition and the design of biomolecular assemblies.
  • Synergistic effects, like H-bond enhanced X-bonds, demonstrate potential for fine-tuning protein properties.

Conclusions:

  • Nonclassical noncovalent interactions are critical for understanding and designing protein stability, assembly, and catalysis.
  • The σ-hole concept provides a framework for utilizing a broader range of noncovalent interactions in protein engineering.
  • Exploiting synergistic ncNC interactions offers promising strategies for developing advanced functional proteins.