Complexo proteico: Diferenzas entre revisións

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Miguelferig (conversa | contribucións)
Miguelferig (conversa | contribucións)
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== Ensamblaxe ==
 
ProperA assemblycorrecta ofensamblaxe multiproteinde complexescomplexos ismultiproteicos importanté moiimportante, sincexa que se é misassemblydeficiente canas leadconsecuencias topoden disastrousser consequencesdesastrosas.<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> In order to study pathway assembly, researchers look at intermediate steps in the pathway. One such technique that allows one to do that is [[electrospray mass spectrometry]], which can identify different intermediate states simultaneously. This has led to the discovery that most complexes follow an ordered assembly pathway.<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> In the cases where disordered assembly is possible, the change from an ordered to a disordered state leads to a transition from function to dysfunction of the complex, since disordered assembly leads to aggregation.<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>
 
The structure of proteins play a role in how the multiprotein complex assembles. The interfaces between proteins can be used to predict assembly pathways.<ref name = "pmid23582331"/> The intrinsic flexibility of proteins also plays a role: more flexible proteins allow for a greater surface area available for interaction.<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>