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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...
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,...
Mechanical Protein Functions01:58

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 

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Related Experiment Video

Updated: Jun 22, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

Understanding biophysicochemical interactions at the nano-bio interface.

Andre E Nel1, Lutz Mädler, Darrell Velegol

  • 1Division of NanoMedicine, David Geffen School of Medicine and California NanoSystems Institute at UCLA, Los Angeles, California 90095, USA. anel@mednet.ucla.edu

Nature Materials
|June 16, 2009
PubMed
Summary

Engineered nanomaterials interact with biological systems, forming interfaces that influence outcomes. Understanding these nanoparticle/biological interactions is key to ensuring the safe use of nanomaterials.

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Capturing the Interaction Kinetics of an Ion Channel Protein with Small Molecules by the Bio-layer Interferometry Assay
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Capturing the Interaction Kinetics of an Ion Channel Protein with Small Molecules by the Bio-layer Interferometry Assay

Published on: March 7, 2018

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Last Updated: Jun 22, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

Capturing the Interaction Kinetics of an Ion Channel Protein with Small Molecules by the Bio-layer Interferometry Assay
10:41

Capturing the Interaction Kinetics of an Ion Channel Protein with Small Molecules by the Bio-layer Interferometry Assay

Published on: March 7, 2018

Area of Science:

  • Nanotechnology
  • Biophysics
  • Materials Science

Background:

  • The rapid advancement of nanotechnology increases human and environmental exposure to engineered nanomaterials.
  • Nanoparticle interactions with biological components create complex nanoparticle/biological interfaces.

Purpose of the Study:

  • To investigate the dynamic biophysicochemical interactions at nanoparticle/biological interfaces.
  • To understand how these interactions influence biocompatible or bioadverse outcomes.
  • To establish predictive structure-activity relationships for nanomaterial safety.

Main Methods:

  • Studying nanoparticle interactions with proteins, membranes, cells, DNA, and organelles.
  • Analyzing the formation of protein coronas, particle wrapping, and intracellular uptake.
  • Investigating biomolecular effects on nanomaterial surface properties, including phase transformations and dissolution.

Main Results:

  • Nanoparticle/biological interfaces are governed by colloidal forces and dynamic biophysicochemical interactions.
  • These interactions can lead to outcomes ranging from biocompatible to bioadverse.
  • Biomolecules can induce significant changes at the nanomaterial surface.

Conclusions:

  • Probing nanoparticle/biological interfaces is crucial for understanding nanomaterial behavior.
  • Nanomaterial properties (size, shape, surface chemistry, coatings) dictate interface activity.
  • This knowledge is essential for the safe application and use of nanomaterials.