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Related Concept Videos

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,...
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...

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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Updates to Guidance on Using Biacore for Protein-Protein Interactions Analysis.

Hui Ma1, Stephen Hearty2, Paul Leonard3

  • 1School of Biochemistry & Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland.

Methods in Molecular Biology (Clifton, N.J.)
|May 13, 2026
PubMed
Summary
This summary is machine-generated.

This guide provides essential tools for Biacore users to design and execute kinetic experiments. It details methods for characterizing antibody fragments from crude lysates, crucial for therapeutic and diagnostic reagent development.

Keywords:
AnalysisAntibodyBiacoreBiosensorInteractionsKineticsPlasmonProtein–proteinResonanceSurface

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

Published on: February 18, 2014

Area of Science:

  • Biophysics
  • Biochemistry
  • Analytical Chemistry

Background:

  • Optical biosensors are vital for studying macromolecular interactions and characterizing biophysical properties of reagents.
  • The vast number of Biacore publications necessitates clear guidance for new users.
  • Kinetic screening assays demand rigorous sample preparation and purification.

Purpose of the Study:

  • To equip Biacore users with the necessary tools for designing and executing kinetic experiments.
  • To provide guidance on basic theory, system maintenance, and assay setup.
  • To offer practical tips for successful Biacore-based studies.

Main Methods:

  • Describes kinetic characterization of single-chain Fv (scFv) antibody fragments from crude bacterial lysates.
  • Utilizes an antibody affinity capture approach for sample preparation.
  • Employs HA-tagged scFv fragments captured by anti-HA tag monoclonal antibodies on a Biacore surface.

Main Results:

  • Demonstrates a protocol for kinetic characterization of antibody fragments directly from crude lysates.
  • Highlights the importance of rigorous sample preparation for kinetic assays.
  • Validates the universal applicability of the described methodologies for various affinity pairs and Biacore systems.

Conclusions:

  • The presented methodologies are universally applicable for kinetic analysis using Biacore systems.
  • Effective sample preparation is key to successful kinetic characterization of biomolecular interactions.
  • This protocol facilitates the study of potential therapeutic and diagnostic reagents.