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Related Concept Videos

Protein Networks02:26

Protein Networks

4.0K
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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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Updated: Jul 31, 2025

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR
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Surface Plasmon Resonance Analysis for Quantifying Protein-Carbohydrate Interactions.

Marie Sofie Møller1, Darrell W Cockburn2, Casper Wilkens3

  • 1Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.

Methods in Molecular Biology (Clifton, N.J.)
|May 6, 2023
PubMed
Summary

Surface Plasmon Resonance (SPR) analysis is a key method for studying protein-carbohydrate interactions. This guide details SPR steps to ensure reliable and reproducible binding affinity results.

Keywords:
BiosensorCarbohydrate-active enzymeCarbohydrate-binding moduleEnzymeProtein-carbohydrate interactionsSurface plasmon resonance

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Biophysics

Background:

  • Surface Plasmon Resonance (SPR) has become a vital technique over the last 20 years for investigating molecular interactions.
  • Commercial SPR instruments are widely available, facilitating its use in various research settings.

Purpose of the Study:

  • To provide a comprehensive overview of Surface Plasmon Resonance (SPR) analysis for protein-carbohydrate interactions.
  • To highlight critical considerations for experimental design to ensure reliable and reproducible results.
  • To guide practitioners through each stage of SPR analysis, from sample immobilization to data interpretation.

Main Methods:

  • Overview of the SPR experimental workflow.
  • Discussion of immobilization strategies for analytes.
  • Guidance on data acquisition and kinetic analysis.
  • Considerations for avoiding common pitfalls in SPR experiments.

Main Results:

  • SPR enables the determination of binding affinities across a wide range (nM to mM).
  • Careful experimental design is crucial to overcome inherent challenges in SPR analysis.
  • The presented considerations facilitate the achievement of trustworthy and repeatable SPR data.

Conclusions:

  • Surface Plasmon Resonance (SPR) is a powerful tool for characterizing protein-carbohydrate interactions.
  • Adherence to best practices in experimental design and data analysis is essential for successful SPR studies.
  • This overview aims to enhance the reliability and reproducibility of SPR-based binding affinity measurements.