Editing Protein complex (section)

== Structure determination ==

The [[molecular structure]] of protein complexes can be determined by experimental techniques such as [[X-ray crystallography]], [[Single particle analysis]] or [[nuclear magnetic resonance]]. Increasingly the theoretical option of [[protein–protein docking]] is also becoming available. One method that is commonly used for identifying the meomplexes{{Clarify|What is this term|date=May 2017}} is [[immunoprecipitation]]. Recently, Raicu and coworkers developed a method to determine the quaternary structure of protein complexes in living cells. This method is based on the determination of pixel-level [[Förster resonance energy transfer]] (FRET) efficiency in conjunction with spectrally resolved [[two-photon microscope]]. The distribution of FRET efficiencies are simulated against different models to get the geometry and stoichiometry of the complexes.<ref>{{ cite journal | author = Raicu V, Stoneman MR, Fung R, Melnichuk M, Jansma DB, Pisterzi LF, Rath S, Fox, M, Wells, JW, Saldin DK | year = 2008 | title = Determination of supramolecular structure and spatial distribution of protein complexes in living cells. | journal = Nature Photonics | volume =  3 | issue = 2 | pages = 107–113 | doi = 10.1038/nphoton.2008.291 }}</ref>