Measuring Protein Interactions by Optical Biosensors

Huaying Zhao1, Lisa F. Boyd1, Peter Schuck1

1 National Institutes of Health, Bethesda, Maryland
Publication Name:  Current Protocols in Protein Science
Unit Number:  Unit 20.2
DOI:  10.1002/cpps.31
Online Posting Date:  April, 2017
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Abstract

This unit gives an introduction to the basic techniques of optical biosensing for measuring equilibrium and kinetics of reversible protein interactions. Emphasis is placed on description of robust approaches that will provide reliable results with few assumptions. How to avoid the most commonly encountered problems and artifacts is also discussed. © 2017 by John Wiley & Sons, Inc.

Keywords: protein interactions; surface plasmon resonance; biolayer interferometry; optical biosensor

     
 
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Table of Contents

  • Introduction
  • Strategic Planning
  • Immobilization Protocols
  • Binding Experiments and Data Analysis
  • Common Experimental Obstacles
  • Summary
  • Acknowledgements
  • Literature Cited
  • Figures
  • Tables
     
 
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Materials

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Figures

Videos

Literature Cited

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Key References
  Davis et al., 1998. See above.
  Contains a detailed description of analyte aggregation effects on the measured surface binding.
  Nieba et al., 1996. See above.
  Demonstration how competition approaches can be used to circumvent kinetic artifacts.
  O'Shannessy et al., 1992. See above.
  Collection of immobilization techniques.
  Schuck, 1997b. See above.
  General review of the method and its application.
  Svittel et al., 2003 and 2007. See above.
  Description of the EVILFIT analysis method.
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