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Protein quaternary structure
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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 = 57β64 | 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.
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