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Methods for the Detection and Analysis of Protein–protein Interactions by Tord Berggård; Sara Linse; Peter James is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract 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.

Who reads Methods for the Detection and Analysis of Protein–protein Interactions?

Author

Tord Berggård; Sara Linse; Peter James

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley; Research Square (ISSN 1615-9853)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)