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Methods for the detection and analysis of protein-protein interactions

  • Tord Berggård
  • Sara Linse
  • Peter James
Publishing year: 2007
Language: English
Pages: 2833-2842
Publication/Series: Proteomics
Volume: 7
Issue: 16
Document type: Journal article review
Publisher: John Wiley & Sons

Abstract english

A large number of methods have been developed over the years to study protein-protein interactions. Many of these techniques are now available to the nonspecialist researcher thanks to new affordable instruments and/or resource centres. A typical protein-protein interaction study usually starts with an initial screen for novel binding partners. We start this review by describing three techniques that can be used for this purpose: (i) affinity-tagged proteins (ii) the two-hybrid system and (iii) some quantitative proteomic techniques that can be used in combination with, e.g., affinity chromatography and coimmunoprecipitation for screening of protein-protein interactions. We then describe some public protein-protein interaction databases that can be searched to identify previously reported interactions for a given bait protein. Four strategies for validation of protein-protein interactions are presented: confocal microscopy for intracellular colocalization of proteins, coimmunoprecipitation, surface plasmon resonance (SPR) and spectroscopic studies. Throughout the review we focus particularly on the advantages and limitations of each method.


  • Industrial Biotechnology
  • Immunology in the medical area
  • affinity tags
  • protein-protein interactions
  • purification
  • protein
  • protein complexes


  • ISSN: 1615-9861
Peter James
E-mail: peter [dot] james [at] immun [dot] lth [dot] se


Department of Immunotechnology

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