title: The effect of a macrocyclic constraint on electron transfer in helical peptides: a step towards tunable molecular wires.
abstract: Two 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.
authors.affiliation: School of Chemistry and Physics, The University of Adelaide, Adelaide, SA 5005, Australia. jingxian.yu@adelaide.edu.au andrew.abell@adelaide.edu.au.
authors.forename: Jingxian
authors.initials: J
authors.lastname: Yu
authors.forename: John R
authors.initials: JR
authors.lastname: Horsley
authors.forename: Katherine E
authors.initials: KE
authors.lastname: Moore
authors.forename: Joe G
authors.initials: JG
authors.lastname: Shapter
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Abell
mesh_terms: D004563:Electrochemistry; D004579:Electron Transport; D006860:Hydrogen Bonding; D047028:Macrocyclic Compounds / Q000737:chemistry*; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D047028:Macrocyclic Compounds; D010455:Peptides