Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 137, Issue 30, Pages 9617-9626Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b03933
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Funding
- Minerva Foundation, Munich
- Nancy and Stephen Grand Centre for Sensors and Security
- Kimmelman center for Biomolecular Structure and Assembly
- Israel Science Foundation
- European Research Council
- Lise Meitner Minerva Center for Computational Chemistry
- Israeli Ministry of Science
- European Union [298664]
- Israel Academy of Sciences and Humanities
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Many novel applications in bioelectronits rely on the interaction between biomolecules and electronically conducting substrates. However, crucial knowledge about the relation between electronic transport via peptides and their amino-acid composition is still absent. Here, we report results of electronic transport measurements via several homopeptides as a function of their structural properties and temperature We demonstrate that the conduction through the peptide depends on its length and secondary Structure as well as on the nature of the constituent amino acid and charge of its residue. We support our experimental observations with high-level electronic structure calculations and suggest off-resonance tunneling as the dominant conduction mechanism via extended peptides. Our findings indicate that both peptide composition and structure of electronic transport across peptides. can affect the efficiency
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