From Experimental Approaches to Computational Techniques: A Review on the Prediction of Protein-Protein Interactions

Table 1

A description of small-scale experimental methods applied to identify PPIs. A description and application of each method and reference to each technique are described below.

Technique	Description	Reference
Co-immunoprecipitations	To determine if two or more proteins are interacting, a purification procedure is applied to identify unknown or novel interactions	[28]
Surface Plasmon Resonance	A bait protein is attached to a gold surface where a laser light is reflected to measure small changes related to protein binding to identify unknown or novel interactions	[29]
Nuclear Magnetic Resonance (NMR)	Provides a dynamic view of PPIs when in a solution to investigate PPIs at the atomic level (i.e., smallest particle)	[30]
X-ray Crystallography	Aids in defining the structure of the interaction through crystallisation of the PPIs to investigate PPIs at an atomic level	[31]
Label Transfer	A known protein is “tagged”. Interactions with this protein are obtained from detecting the tag to verify predicted or known PPIs	[32]
FRET	Proteins are labelled with fluorescence to detect interacting proteins to verify predicted or known PPIs	[32]
Far Western Blot	Proteins are applied to the blot to detect proteins of interest to verify predicted or known PPIs	[31]