Show simple item record

dc.contributor.authorMozo Villarías, Angel
dc.contributor.authorCedano, Juan
dc.contributor.authorQuerol, Enrique
dc.date.accessioned2016-05-09T10:10:34Z
dc.date.issued2016
dc.identifier.issn0175-7571
dc.identifier.urihttp://hdl.handle.net/10459.1/56995
dc.description.abstractThis article describes the formation of homodimers from their constituting monomers, based on the rules set by a simple model of electric and hydrophobic interactions. These interactions are described in terms of the electric dipole moment (D) and hydrophobic moment vectors (H) of proteins. The distribution of angles formed by the two dipole moments of monomers constituting dimers were analysed, as well as the distribution of angles formed by the two hydrophobic moments. When these distributions were fitted to Gaussian curves, it was found that for biological dimers, the D vectors tend mostly to adopt a perpendicular arrangement with respect to each other, in which the constituting dipoles have the least interaction. A minor population tends towards an antiparallel arrangement implying maximum electric attraction. Also in biological dimers, the H vectors of most monomers tend to interact in such a way that the total hydrophobic moment of the dimer increases with respect to those of the monomers. This shows that hydrophobic moments have a tendency to align. In dimers originating in the crystallisation process, the distribution of angles formed by both hydrophobic and electric dipole moments appeared rather featureless, probably because of unspecific interactions in the crystallisation processes. The model does not describe direct interactions between H and D vectors although the distribution of angles formed by both vectors in dimers was analysed. It was found that in most cases these angles tended to be either small (both moments aligned parallel to each other) or large (antiparallel disposition).ca_ES
dc.description.sponsorshipThis research was supported by Ministerio de Ciencia e Innovación of Spain [BIO2013-48704-R and BFU2013- 50176-EXP], the Centre de Referència de R + D de Biotecnologia de la Generalitat de Catalunya and the Comisión Coordinadora del Interior de Uruguay.
dc.language.isoengca_ES
dc.publisherSpringerca_ES
dc.relationMINECO/PN2013-2016/BIO2013-48704-R
dc.relationMINECO/PN2013-2016/BFU2013-50176-EXP
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1007/s00249-015-1100-3ca_ES
dc.relation.ispartofEuropean Biophysics Journal, 2016, vol. 45, núm. 4, p. 341–346ca_ES
dc.rights(c) Springer, 2016ca_ES
dc.subjectProtein monomerca_ES
dc.subjectProtein dimerca_ES
dc.subjectElectric dipole momentca_ES
dc.subjectHydrophobic momentca_ES
dc.titleVector description of electric and hydrophobic interactions in protein homodimersca_ES
dc.typearticleca_ES
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccessca_ES
dc.identifier.doihttps://doi.org/10.1007/s00249-015-1100-3
dc.date.embargoEndDate2025-01-01


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record