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March 1, 1995Microbiological ReviewsOpen Access

Protein-protein interactions: methods for detection and analysis

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Authors

EPEric M. PhizickySFStanley Fields

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Overview

Methodological review details biochemical, molecular, and genetic approaches to analyze protein binding and affinities, highlighting technical advantages and analytical challenges across...

Key Points

  • To provide a comprehensive, practical guide evaluating biochemical, molecular biological, and genetic strategies for identifying protein-protein interactions and measuring quantitative binding affinities.
  • Reviewed qualitative biochemical detection assays, including protein affinity chromatography, affinity blotting, coimmunoprecipitation, and chemical cross-linking.
  • Evaluated molecular and genetic screening strategies, including yeast two-hybrid systems, phage display, and extragenic suppressor mutant isolation.
  • Assessed quantitative equilibrium binding approaches, such as sedimentation, gel filtration, fluorescence-based assays, and surface plasmon resonance.
  • Identified distinct technical advantages, limitations, and potential experimental artifacts associated with in vitro and in vivo interaction mapping techniques.
  • Demonstrated multi-method application frameworks through three well-characterized domain models engaged in complex macromolecular interactions.

Cite This Study

Phizicky et al. (1995) studied this question.

synapsesocial.com/papers/6a799b9efb5b6b43000dbff3https://doi.org/10.1128/mr.59.1.94-123.1995
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