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Understanding membrane protein folding and interfaciality

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Understanding membrane protein folding and interfaciality

dc.contributor.advisor	Mingarro Muñoz, Ismael
dc.contributor.advisor	Martínez Gil, Luis
dc.contributor.author	Grau, Brayan
dc.contributor.other	Departament d'Algebra	es_ES
dc.date.accessioned	2021-03-06T10:46:00Z
dc.date.available	2021-09-03T04:45:05Z
dc.date.issued	2021	es_ES
dc.date.submitted	01-03-2021	es_ES
dc.identifier.uri	https://hdl.handle.net/10550/78166
dc.description.abstract	Despite the bast abundance of membrane proteins encoded in the human genome, the understanding of their biosynthesis and folding is far from the knowledge we have of soluble proteins. In the present thesis the main objective is to increase our knowledge on membrane protein biogenesis and folding, from the first steps of folding within the ribosome to the native structure acquisition in the membrane. Hydrophobicity, helicity and length of the polypeptide chain have been stablished as the major determinants for alpha-helical conformation adoption within the ribosome exit tunnel. Also, a 'biological' interfacial scale for the 20 naturally occurring amino acids were determined due to the development of the Lep3G assay. This scale is important to deeply study the membrane interface contribution to the membrane protein integration since not all membrane proteins across the membrane, but some keep anchored to one layer. Concerning to the membrane packing, an exhaustive analysis of hydrophobic matching between largely different hydrophobic region in cells has been done for the first time. We confirmed that, in living cells, adaptations in both, the membrane thickness and transmembrane domain tilting, enable helix-helix packing besides length differences between both. Finally, we determined once again that the final topology acquisition is not only guided by the hydrophobicity of the transmembrane domains which compose the protein, but also by packing between transmembrane helices and the presence of specialized connecting loops.	es_ES
dc.format.extent	215 p.	es_ES
dc.language.iso	en_US	es_ES
dc.subject	membrane	es_ES
dc.subject	protein	es_ES
dc.subject	interfacial	es_ES
dc.subject	hydrophobic	es_ES
dc.subject	matching	es_ES
dc.subject	folding	es_ES
dc.title	Understanding membrane protein folding and interfaciality	es_ES
dc.type	doctoral thesis	es_ES
dc.subject.unesco	UNESCO::CIENCIAS DE LA VIDA	es_ES
dc.embargo.terms	6 months	es_ES