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Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/82878
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dc.contributor.authorYu, J.-
dc.contributor.authorHorsley, J.-
dc.contributor.authorMoore, K.-
dc.contributor.authorShapter, J.-
dc.contributor.authorAbell, A.-
dc.date.issued2014-
dc.identifier.citationChemical Communications, 2014; 50(14):1652-1654-
dc.identifier.issn1359-7345-
dc.identifier.issn1364-548X-
dc.identifier.urihttp://hdl.handle.net/2440/82878-
dc.description.abstractTwo helical peptides, one constrained by a covalent side-chain staple, exhibit vastly different electronic properties despite adopting essentially the same backbone conformation. High level calculations confirm that these differences are due to the additional backbone rigidity imparted by the macrocyclic constraint.-
dc.description.statementofresponsibilityJingxian Yu, John R. Horsley, Katherine E. Moore, Joe G . Shapter and Andrew D. Abell-
dc.language.isoen-
dc.publisherRoyal Society of Chemistry-
dc.rightsThe journal © The Royal Society of Chemistry 2014-
dc.source.urihttp://dx.doi.org/10.1039/c3cc47885h-
dc.subjectMacrocyclic Compounds-
dc.subjectPeptides-
dc.subjectProtein Structure, Secondary-
dc.subjectElectron Transport-
dc.subjectElectrochemistry-
dc.subjectHydrogen Bonding-
dc.subjectModels, Molecular-
dc.titleThe effect of a macrocyclic constraint on electron transfer in helical peptides: a step towards tunable molecular wires-
dc.typeJournal article-
dc.contributor.organisationInstitute for Photonics & Advanced Sensing (IPAS)-
dc.identifier.doi10.1039/C3CC47885H-
pubs.publication-statusPublished-
dc.identifier.orcidYu, J. [0000-0002-6489-5988]-
dc.identifier.orcidAbell, A. [0000-0002-0604-2629]-
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IPAS publications

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