NAGIOS: RODERIC FUNCIONANDO

Charge Pair Interactions in Transmembrane Helices and Turn Propensity of the Connecting Sequence Promote Helical Hairpin Insertion

Repositori DSpace/Manakin

IMPORTANT: Aquest repositori està en una versió antiga des del 3/12/2023. La nova instal.lació está en https://roderic.uv.es/

Charge Pair Interactions in Transmembrane Helices and Turn Propensity of the Connecting Sequence Promote Helical Hairpin Insertion

dc.contributor.author	Bañó Polo, Manuel
dc.contributor.author	Martínez Gil, Luis
dc.contributor.author	Wallner, Björn
dc.contributor.author	Nieva, José Luis
dc.contributor.author	Elofsson, Arne
dc.contributor.author	Mingarro Muñoz, Ismael
dc.date.accessioned	2016-09-21T14:06:52Z
dc.date.available	2016-09-21T14:06:52Z
dc.date.issued	2013
dc.identifier.citation	Bañó Polo, Manuel Martínez Gil, Luis Wallner, Björn Nieva, José Luis Elofsson, Arne Mingarro Muñoz, Ismael 2013 Charge Pair Interactions in Transmembrane Helices and Turn Propensity of the Connecting Sequence Promote Helical Hairpin Insertion Journal of Molecular Biology 425 4 830 840
dc.identifier.uri	http://hdl.handle.net/10550/55076
dc.description.abstract	α-Helical hairpins, consisting of a pair of closely spaced transmembrane (TM) helices that are connected by a short interfacial turn, are the simplest structural motifs found in multi-spanning membrane proteins. In naturally occurring hairpins, the presence of polar residues is common and predicted to complicate membrane insertion. We postulate that the pre-packing process offsets any energetic cost of allocating polar and charged residues within the hydrophobic environment of biological membranes. Consistent with this idea, we provide here experimental evidence demonstrating that helical hairpin insertion into biological membranes can be driven by electrostatic interactions between closely separated, poorly hydrophobic sequences. Additionally, we observe that the integral hairpin can be stabilized by a short loop heavily populated by turn-promoting residues. We conclude that the combined effect of TM¿TM electrostatic interactions and tight turns plays an important role in generating the functional architecture of membrane proteins and propose that helical hairpin motifs can be acquired within the context of the Sec61 translocon at the early stages of membrane protein biosynthesis. Taken together, these data further underline the potential complexities involved in accurately predicting TM domains from primary structures.
dc.language.iso	eng
dc.relation.ispartof	Journal of Molecular Biology, 2013, vol. 425, num. 4, p. 830-840
dc.subject	Proteïnes de membrana
dc.subject	Bioquímica
dc.title	Charge Pair Interactions in Transmembrane Helices and Turn Propensity of the Connecting Sequence Promote Helical Hairpin Insertion
dc.type	journal article	es_ES
dc.date.updated	2016-09-21T14:06:52Z
dc.identifier.doi	10.1016/j.jmb.2012.12.001
dc.identifier.idgrec	083227
dc.rights.accessRights	open access	es_ES