Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/82878
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Type: Journal article
Title: The effect of a macrocyclic constraint on electron transfer in helical peptides: a step towards tunable molecular wires
Author: Yu, J.
Horsley, J.
Moore, K.
Shapter, J.
Abell, A.
Citation: Chemical Communications, 2014; 50(14):1652-1654
Publisher: Royal Society of Chemistry
Issue Date: 2014
ISSN: 1359-7345
1364-548X
Organisation: Institute for Photonics & Advanced Sensing (IPAS)
Statement of
Responsibility: 
Jingxian Yu, John R. Horsley, Katherine E. Moore, Joe G . Shapter and Andrew D. Abell
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.
Keywords: Macrocyclic Compounds; Peptides; Protein Structure, Secondary; Electron Transport; Electrochemistry; Hydrogen Bonding; Models, Molecular
Rights: The journal © The Royal Society of Chemistry 2014
RMID: 0030000083
DOI: 10.1039/C3CC47885H
Appears in Collections:IPAS publications

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