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dc.contributor.authorNieto Ortega, Belén
dc.contributor.authorNebot Carda, Vicent J.
dc.contributor.authorMiravet, Juan
dc.contributor.authorEscuder, Beatriu
dc.contributor.authorLópez Navarrete, Juan T.
dc.contributor.authorCasado, Juan
dc.contributor.authorRamírez, Francisco J.
dc.date.accessioned2013-06-14T12:01:33Z
dc.date.available2013-06-14T12:01:33Z
dc.date.issued2012
dc.identifier.issn1948-7185
dc.identifier.urihttp://hdl.handle.net/10234/67198
dc.description.abstractWe elucidate the supramolecular organization in the form of microsize fibrils of gels formed by a l-Valine peptidomimetic compound. Analysis was based on circular dichroism spectroscopies, vibrational (VCD) and electronic (CD), supported by microscopy (atomic force and scanning electron). We show how the VCD spectra give account of the micrometric structure of the fibrils formed by the helicoidal arrangement of simpler proto-fibrils, which are organized in a lower hierarchical level. This ability is used to monitorize a fully reversible change in the handedness of the helix by modulating different external stimuli as pH or ionic strength, thus providing the first observation by VCD of such a phenomenon in a short peptide.ca_CA
dc.format.extent4 p.ca_CA
dc.language.isoengca_CA
dc.publisherAmerican Chemical Societyca_CA
dc.rightsCopyright © 2012 American Chemical Societyca_CA
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/*
dc.subjectcircular dichroismca_CA
dc.subjectmicroscopyca_CA
dc.subjecthydrogelca_CA
dc.subjectchiralityca_CA
dc.subjectpeptidomimeticca_CA
dc.titleVibrational Circular Dichroism Shows Reversible Helical Handedness Switching in Peptidomimetic l-Valine Fibrilsca_CA
dc.typeinfo:eu-repo/semantics/articleca_CA
dc.identifier.doihttp://dx.doi.org/10.1021/jz300725d
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccessca_CA
dc.relation.publisherVersionhttp://pubs.acs.org/doi/abs/10.1021%2Fjz300725dca_CA


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