title: Cold denaturation induces inversion of dipole and spin transfer in chiral peptide monolayers.
abstract: Chirality-induced spin selectivity is a recently-discovered effect, which results in spin selectivity for electrons transmitted through chiral peptide monolayers. Here, we use this spin selectivity to probe the organization of self-assembled α-helix peptide monolayers and examine the relation between structural and spin transfer phenomena. We show that the α-helix structure of oligopeptides based on alanine and aminoisobutyric acid is transformed to a more linear one upon cooling. This process is similar to the known cold denaturation in peptides, but here the self-assembled monolayer plays the role of the solvent. The structural change results in a flip in the direction of the electrical dipole moment of the adsorbed molecules. The dipole flip is accompanied by a concomitant change in the spin that is preferred in electron transfer through the molecules, observed via a new solid-state hybrid organic-inorganic device that is based on the Hall effect, but operates with no external magnetic field or magnetic material.
authors.affiliation: Department of Chemical Physics, Weizmann Institute of Science, Rehovoth 76100, Israel.
authors.forename: Meital
authors.initials: M
authors.lastname: Eckshtain-Levi
authors.affiliation: Department of Chemical Physics, Weizmann Institute of Science, Rehovoth 76100, Israel.
authors.forename: Eyal
authors.initials: E
authors.lastname: Capua
authors.affiliation: Department of Materials and Interfaces, Weizmann Institute of Science, Rehovoth 76100, Israel.
authors.forename: Sivan
authors.initials: S
authors.lastname: Refaely-Abramson
authors.affiliation: Department of Materials and Interfaces, Weizmann Institute of Science, Rehovoth 76100, Israel.
authors.forename: Soumyajit
authors.initials: S
authors.lastname: Sarkar
authors.affiliation: Department of Structural Biology, Weizmann Institute of Science, Rehovoth 76100, Israel.
authors.forename: Yulian
authors.initials: Y
authors.lastname: Gavrilov
authors.affiliation: Department of Chemical Physics, Weizmann Institute of Science, Rehovoth 76100, Israel.
authors.forename: Shinto P
authors.identifier: http://orcid.org/0000-0001-6851-0785
authors.initials: SP
authors.lastname: Mathew
authors.affiliation: Department of Applied Physics and Center for Nano Science and Nanotechnology, The Hebrew University, Jerusalem 91904, Israel.
authors.forename: Yossi
authors.initials: Y
authors.lastname: Paltiel
authors.affiliation: Department of Structural Biology, Weizmann Institute of Science, Rehovoth 76100, Israel.
authors.forename: Yaakov
authors.initials: Y
authors.lastname: Levy
authors.affiliation: Department of Materials and Interfaces, Weizmann Institute of Science, Rehovoth 76100, Israel.
authors.forename: Leeor
authors.initials: L
authors.lastname: Kronik
authors.affiliation: Department of Chemical Physics, Weizmann Institute of Science, Rehovoth 76100, Israel.
authors.forename: Ron
authors.initials: R
authors.lastname: Naaman
mesh_terms: D000409:Alanine; D000621:Aminoisobutyric Acids; D003080:Cold Temperature; D004579:Electron Transport; D004583:Electrons; D056004:Molecular Dynamics Simulation; D009842:Oligopeptides / Q000737:chemistry*; D011489:Protein Denaturation; D017433:Protein Structure, Secondary
chemical_list: D000621:Aminoisobutyric Acids; D009842:Oligopeptides; D000409:Alanine