Editing Interactome (section)

==Experimental methods to map interactomes==
The study of interactomes is called interactomics. The basic unit of a protein network is the protein–protein interaction (PPI). While there are numerous methods to study PPIs, there are relatively few that have been used on a large scale to map whole interactomes.

The [[Two-hybrid screening|yeast two hybrid]] system (Y2H) is suited to explore the binary interactions among two proteins at a time. Affinity purification and subsequent mass spectrometry is suited to identify a protein complex. Both methods can be used in a high-throughput (HTP) fashion. Yeast two hybrid screens allow false positive interactions between proteins that are never expressed in the same time and place; affinity capture mass spectrometry does not have this drawback, and is the current gold standard. Yeast two-hybrid data better indicates non-specific tendencies towards sticky interactions rather while affinity capture mass spectrometry better indicates functional in vivo protein–protein interactions.<ref>{{cite journal|last=Brettner|first=Leandra M.|author2=Joanna Masel|title=Protein stickiness, rather than number of functional protein–protein interactions, predicts expression noise and plasticity in yeast|journal=BMC Systems Biology|year=2012|volume=6|pages=128|doi=10.1186/1752-0509-6-128|pmid=23017156|pmc=3527306 |doi-access=free }} {{open access}}</ref><ref name="10.3389/fnmol.2014.00058">{{cite journal |last=Mukherjee |first=K |author2=Slawson |author3=Christmann |author4=Griffith |date=June 2014 |title=Neuron-specific protein interactions of Drosophila CASK-ß are revealed by mass spectrometry |journal=Front. Mol. Neurosci. |volume= 7|pages= 58| pmid =25071438|doi = 10.3389/fnmol.2014.00058 | pmc=4075472|doi-access=free }}</ref>