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

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

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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.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.rights.uri info:eu-repo/semantics/openAccess
dc.source 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.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 info:eu-repo/semantics/article
dc.date.updated 2016-09-21T14:06:52Z
dc.identifier.doi http://dx.doi.org/10.1016/j.jmb.2012.12.001
dc.identifier.idgrec 083227

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