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Protein-protein interactions: methods for detection and analysis.

Open access
Phizicky, E M, Fields, S·1995·Microbiological reviews

Abstract

The function and activity of a protein are often modulated by other proteins with which it interacts. This review is intended as a practical guide to the analysis of such protein-protein interactions. We discuss biochemical methods such as protein affinity chromatography, affinity blotting, coimmunoprecipitation, and cross-linking; molecular biological methods such as protein probing, the two-hybrid system, and phage display: and genetic methods such as the isolation of extragenic suppressors, synthetic mutants, and unlinked noncomplementing mutants. We next describe how binding affinities can be evaluated by techniques including protein affinity chromatography, sedimentation, gel filtration, fluorescence methods, solid-phase sampling of equilibrium solutions, and surface plasmon resonance. Finally, three examples of well-characterized domains involved in multiple protein-protein interactions are examined. The emphasis of the discussion is on variations in the approaches, concerns in evaluating the results, and advantages and disadvantages of the techniques.

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Crossref · 10.1128/mmbr.59.1.94-123.1995

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Metadata

Authors
Phizicky, E. M., & Fields, S.
Venue
Microbiological reviews
Published
1995
Volume
59
Issue
1
Pages
94-123
ISSN
0146-0749 (ISSN-L)
OpenAlex
W2130832525
Cited by
966
References
6
FWCI
18.66
Type
journal article
Language
en
Open access
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CoChat. (2026). Citation check: Protein-protein interactions: methods for detection and analysis. https://app.cochat.ai/papers/10.1128/mmbr.59.1.94-123.1995
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Phizicky, E. M., & Fields, S. (1995). Protein-protein interactions: methods for detection and analysis. Microbiological reviews. https://doi.org/10.1128/mmbr.59.1.94-123.1995

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