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* Surface-induced dissociation mass spectrometry<ref name = "Stiving_2019">{{cite journal | vauthors = Stiving AQ, VanAernum ZL, Busch F, Harvey SR, Sarni SH, Wysocki VH | title = Surface-Induced Dissociation: An Effective Method for Characterization of Protein Quaternary Structure | journal = Analytical Chemistry | volume = 91 | issue = 1 | pages = 190–209 | date = January 2019 | pmid = 30412666 | pmc = 6571034 | doi = 10.1021/acs.analchem.8b05071 | department = review }}</ref>
* Coimmunoprecipation<ref name = "Milligan_2005">{{cite journal | vauthors = Milligan G, Bouvier M | title = Methods to monitor the quaternary structure of G protein-coupled receptors | journal = The FEBS Journal | volume = 272 | issue = 12 | pages = 2914–2925 | date = June 2005 | pmid = 15955052 | doi = 10.1111/j.1742-4658.2005.04731.x | s2cid = 23274563 | department = review }}</ref>
* [[Förster resonance energy transfer|FRET]]<ref name = "Milligan_2005" /><ref name = "Raicu_2013">{{cite journal | vauthors = Raicu V, Singh DR | title = FRET spectrometry: a new tool for the determination of protein quaternary structure in living cells | journal = Biophysical Journal | volume = 105 | issue = 9 | pages = 1937–1945 | date = November 2013 | pmid = 24209838 | pmc = 3824708 | doi = 10.1016/j.bpj.2013.09.015 | bibcode = 2013BpJ...105.1937R | department = primary }}</ref>
* Nuclear Magnetic Resonance (NMR)<ref name="Prischi_2016">{{cite journal | vauthors = Prischi F, Pastore A | title = Application of Nuclear Magnetic Resonance and Hybrid Methods to Structure Determination of Complex Systems | journal = Advances in Experimental Medicine and Biology | volume = 896 | issue = | pages = 351–368 | date = 2016 | pmid = 27165336 | doi = 10.1007/978-3-319-27216-0_22 | isbn = 978-3-319-27214-6 | department = review }}</ref><ref name="Wells_2018">{{cite book | vauthors = Wells JN, Marsh JA | title = Protein Complex Assembly | chapter = Experimental Characterization of Protein Complex Structure, Dynamics, and Assembly | series = Methods in Molecular Biology | volume = 1764 | pages = 3–27 | date = 2018 | pmid = 29605905 | doi = 10.1007/978-1-4939-7759-8_1 | isbn = 978-1-4939-7758-1 | quote = Section 4: Nuclear Magnetic Resonance Spectroscopy | department = review }}</ref>
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==Assembly==
Direct interaction of two nascent proteins emerging from nearby [[ribosome]]s appears to be a general mechanism for oligomer formation.<ref name="Bertolini_2021">{{cite journal | vauthors = Bertolini M, Fenzl K, Kats I, Wruck F, Tippmann F, Schmitt J, Auburger JJ, Tans S, Bukau B, Kramer G | display-authors = 6 | title = Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly | journal = Science | volume = 371 | issue = 6524 | pages = 57–64 | date = January 2021 | pmid = 33384371 | doi = 10.1126/science.abc7151 | pmc = 7613021 | bibcode = 2021Sci...371...57B | s2cid = 229935047 | url = https://ir.amolf.nl/pub/10361 | department = primary }}</ref> Hundreds of protein oligomers were identified that assemble in human cells by such an interaction.<ref name="Bertolini_2021" /> The most prevalent form of interaction was between the N-terminal regions of the interacting proteins. Dimer formation appears to be able to occur independently of dedicated assembly machines.
== See also ==
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