A correcta ensamblaxe de complexos multiproteicos é moiimportante, xa que se é deficiente as consecuencias poden ser desastrosas.<ref>{{cite journal|last1=Dobson|first1=Christopher M|title=Protein folding and misfolding|journal=Nature|date=December 2003|volume=426|issue=6968|pages=884–90|doi=10.1038/nature02261|pmid=14685248}}</ref> InPara orderestudas toa studysecuencia pathwayde assemblyesamblaxe, researchersos lookinvestigadores atestudan intermediateos stepspasos inintermedios theda pathway.vía Onede suchesamblaxe. techniqueUnha thattécnica allowsdeste onetipo toé do that isa [[electrosprayespectrometría massde spectrometrymasas electrospray]], whichque canpode identifyidentificar differentdiferentes intermediateestados statesintermedios simultaneouslysimultaneamente. ThisIsto haslevou ledao todescubrimento thede discoveryque thatmoitos mostcomplexos complexesseguen followunha ansecuencia orderedde assemblyensamblaxe pathwayordenada.<ref name = "pmid23582331">{{cite journal | authors = Marsh JA, Hernández H, Hall Z, Ahnert SE, Perica T, Robinson CV, Teichmann SA | title = Protein complexes are under evolutionary selection to assemble via ordered pathways | journal = Cell | volume = 153 | issue = 2 | pages = 461–470 | date = Apr 2013 | pmid = 23582331 | doi = 10.1016/j.cell.2013.02.044 }}</ref> InNos thecasos casesnos whereque disorderedé assemblyposible isunha possibleensamblaxe desordenada, theo changecambio fromdun an ordered toestadoordenado a disorderedun statedesordenado leadsleva too acoplexo transitioná fromtransición functiondesde toa dysfunctionfunción ofá the complexdisfunción, sincexa disorderedque assemblya leadsensamblaxe todesordenada orixina aggregationagregación.<ref>{{cite journal|last1=Sudha|first1=Govindarajan|last2=Nussinov|first2=Ruth|last3=Srinivasan|first3=Narayanaswamy|title=An overview of recent advances in structural bioinformatics of protein-protein interactions and a guide to their principles|journal=Progress in biophysics and molecular biology|volume=116|issue=2-3|pages=141–50|doi=10.1016/j.pbiomolbio.2014.07.004|pmid=25077409}}</ref>
TheA structureestrutura ofdas proteinsproteínas playxoga aun rolepapel innomodo howen theque multiproteinse complexensambla assembleso complexoproteico. TheAs interfaces betweenentre proteinsas canproteínas bepoden usedutilizarse topara predictpredicir assemblyas pathwaysscuencias de ensamblaxe.<ref name = "pmid23582331"/> TheA intrinsicflexibilidade flexibilityintrínseca ofdas proteinsproteínas alsotamén playsxoga aun rolepapel: moreas flexibleproteínas proteinsmáis allowflexibles forpermiten aque greaterse surfacepoida areadispoñen availabledunha formaior área superficial para a interactioninteracción.<ref>{{cite journal|last1=Marsh|first1=Joseph|last2=Teichmann|first2=Sarah A|title=Protein flexibility facilitates quaternary structure assembly and evolution|journal=PLoS biology|date=May 2014|volume=12|issue=5|doi=10.1371/journal.pbio.1001870|pmid=24866000}}</ref>
Aínda que a ensamblaxe é un proceso diferente da desensamblaxe, as dúas son reversibles tanto nos complexos homoméricos coma heteroméricos. Deste xeito, o proceso global pode denominarse (des)ensamblaxe.
While assembly is a different process from disassembly, the two are reversible in both homomeric and heteromeric complexes. Thus, the overall process can be referred to as (dis)assembly.
=== Importancia evolutiva da ensamblaxe de complexos multiproteicos ===
