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Updated: May 16, 2026

Characterizing Single-Molecule Conformational Changes Under Shear Flow with Fluorescence Microscopy
Published on: January 25, 2020
Molecular direction dependence of single-molecule conductance of a helical peptide in molecular junction
Hirotaka Uji1, Tomoyuki Morita, Shunsaku Kimura
1Department of Material Chemistry, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku-Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.
Abstract:
The helix-peptide dipole effect on single-molecule conductance was analysed experimentally and theoretically with a single 8mer helical peptide. The helical peptide was immobilized on a gold surface in two opposite directions of the helix dipole. Single-molecule conductance of the helical peptide was determined to be 2.4 × 10(-5) G(0) by scanning tunneling microscopy (STM) break-junction measurements under the condition of applied bias voltage parallel to the dipole, which was about 1.2-fold larger than that in the anti-parallel direction. Theoretical calculation also supports that the helix dipole influences the electron transport reaction depending on parallel or anti-parallel orientation of the dipole against the applied electric field.
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