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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,...
Drug-Receptor Bonds01:25

Drug-Receptor Bonds

Drug-receptor bonds are formed through various chemical forces when drugs interact with target cells. Covalent bonds, strong and irreversible, are exemplified by DNA-alkylating anticancer agents that inhibit cell division. However, such irreversible drug binding lacks selectivity and can modify the DNA of the surrounding healthy cells. Covalent binding often contributes to tissue toxicity, as seen with chloroform and paracetamol metabolites binding to the liver, causing hepatotoxicity.
In...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

Ultra-weak reversible protein-protein interactions.

Arthur J Rowe1

  • 1University of Nottingham, NCMH, School of Biosciences, Sutton Bonington, Leicestershire LE12 5RD, UK. arthur.rowe@connectfree.co.uk

Methods (San Diego, Calif.)
|February 23, 2011
PubMed
Summary
This summary is machine-generated.

Investigating ultra-weak protein interactions (K(d)>100μM) is crucial for cell biology. This review covers methods like NMR spectroscopy and analytical ultracentrifugation (AUC) for characterizing these weak biological interactions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Ultra-weak protein interactions (K(d)>100μM) are increasingly important in cell biology, particularly for cell-cell interactions and signaling.
  • Quantitative methods for defining these interactions are essential for understanding biological processes.

Purpose of the Study:

  • To review and discuss methods for the quantitative definition of ultra-weak protein interactions.
  • To highlight the capabilities and limitations of various techniques in characterizing weak binding affinities.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy can identify interactions weaker than 3mM and provide structural insights.
  • Analytical Ultracentrifugation (AUC) is a powerful free solution technique capable of characterizing K(d) values up to 50mM.
  • Computational algorithms can remove thermodynamic/hydrodynamic effects complicating AUC data analysis.

Main Results:

  • NMR spectroscopy is effective for detecting and characterizing weak protein interactions.
  • AUC offers high practical capability for quantifying weak interactions, even in the presence of confounding effects.
  • Both velocity and equilibrium AUC approaches have distinct advantages for studying weak protein binding.

Conclusions:

  • Accurate characterization of ultra-weak protein interactions is achievable with advanced biophysical techniques.
  • NMR and AUC are key methods for studying weak protein-protein binding relevant to cellular processes.
  • Further development of computational methods enhances the utility of AUC for weak interaction analysis.