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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

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dc.contributor.author Orzáez Calatayud, María del Mar
dc.contributor.author Lukovic, Dunja
dc.contributor.author Abad Mazario, Concepción
dc.contributor.author Pérez Payá, Enrique
dc.contributor.author Mingarro Muñoz, Ismael
dc.date.accessioned 2018-04-13T14:32:33Z
dc.date.available 2018-04-13T14:32:33Z
dc.date.issued 2005
dc.identifier.citation Orzáez Calatayud, María del Mar Lukovic, Dunja Abad Mazario, Concepción Pérez Payá, Enrique Mingarro Muñoz, Ismael 2005 Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif Febs Letters 579 7 1633 1638
dc.identifier.uri http://hdl.handle.net/10550/65663
dc.description.abstract The principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimer- isation motif that mediates transmembrane (TM) helix associa- tion, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Fur- ther, we have used this minimised GpA motif to assess the influ- ence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix-helix association and/or dissociation between TM fragments.
dc.language.iso eng
dc.relation.ispartof Febs Letters, 2005, vol. 579, num. 7, p. 1633-1638
dc.subject Proteïnes de membrana
dc.title Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif
dc.type journal article es_ES
dc.date.updated 2018-04-13T14:32:33Z
dc.identifier.doi 10.1016/j.febslet.2005.01.078
dc.identifier.idgrec 026410
dc.rights.accessRights open access es_ES

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