Editing Protein complex (section)

=== Fuzzy complex ===
[[Fuzzy complex|Fuzzy protein complexes]] have more than one structural form or dynamic structural disorder in the bound state.<ref name="pmid18054235">{{cite journal |vauthors=Tompa P, Fuxreiter M | title = Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions | journal = Trends Biochem. Sci. | volume = 33 | issue = 1 | pages = 2–8 |date=January 2008 | pmid = 18054235 | doi = 10.1016/j.tibs.2007.10.003 }}</ref> This means that proteins may not fold completely in either transient or permanent complexes. Consequently, specific complexes can have ambiguous interactions, which vary according to the environmental signals. Hence different ensembles of structures result in different (even opposite) biological functions.<ref name="pmid21927770">{{cite journal | author = Fuxreiter M | title = Fuzziness: linking regulation to protein dynamics | journal = Mol Biosyst | volume = 8 | issue = 1 | pages = 168–77 |date=January 2012 | pmid = 21927770 | doi = 10.1039/c1mb05234a }}</ref> Post-translational modifications, protein interactions or alternative splicing modulate the [[conformational ensembles]] of fuzzy complexes, to fine-tune affinity or specificity of interactions. These mechanisms are often used for regulation within the [[eukaryotic transcription]] machinery.<ref name="pmid21620710">{{cite journal |vauthors=Fuxreiter M, Simon I, Bondos S | title = Dynamic protein–DNA recognition: beyond what can be seen | journal = Trends Biochem. Sci. | volume = 36 | issue = 8 | pages = 415–23 |date=August 2011 | pmid = 21620710 | doi = 10.1016/j.tibs.2011.04.006 }}</ref>