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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
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Non-covalent interactions between electroactivated soybean protein isolate and naringin: Structure, functionality and

Qianzhu Qin1, Weining Wang1, Xiue Han1

  • 1School of Food Science, Northeast Agricultural University, Harbin 150030, China.

Food Chemistry
|July 15, 2026
PubMed
Summary

Electroactivation-treated soybean protein isolate (SPI) combined with naringin (NAR) formed stable complexes (EAP-N) with enhanced solubility, antioxidant activity, and improved interfacial properties, showing potential for food applications.

Keywords:
Electroactivation technologyMolecular dockingNaringinNon-covalent complexSoybean protein isolate

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Area of Science:

  • Food Science
  • Biochemistry
  • Materials Science

Background:

  • Soybean protein isolate (SPI) has limited applications.
  • Polyphenols like naringin (NAR) can interact with proteins.
  • Electroactivation (EA) is a novel treatment for protein modification.

Purpose of the Study:

  • To create and characterize protein-polyphenol complexes using electroactivation-treated SPI (EAP) and NAR.
  • To investigate the structural and functional properties of these EAP-N complexes.
  • To explore the potential of EAP-N complexes as functional food ingredients.

Main Methods:

  • Soybean protein isolate (SPI) was treated with electroactivation (EA) to obtain EAP.
  • EAP was combined with naringin (NAR) to form EAP-N complexes.
  • Structural properties (solubility, particle size, zeta potential) and functional properties (antioxidant activity, interfacial properties) were analyzed.
  • Molecular forces and molecular docking were used to study interactions.

Main Results:

  • EA treatment unfolded SPI, reduced particle size, and increased zeta potential.
  • Stable EAP-N complexes were formed, with optimal solubility at 0.6 mg/mL NAR.
  • EAP-N complexes showed enhanced antioxidant activity and improved interfacial properties compared to SPI.
  • Interactions between EAP and NAR were primarily non-covalent (hydrogen bonds, hydrophobic interactions).

Conclusions:

  • EAP-N complexes possess enhanced functional properties compared to native SPI.
  • The interaction mechanism involves non-covalent forces, facilitated by modified EAP.
  • EAP-N complexes show promise as functional ingredients for emulsion and foam-based food systems.