Cold denaturation induces inversion of dipole and spin transfer in chiral peptide monolayers.
Nat Commun
; 7: 10744, 2016 Feb 26.
Article
in En
| MEDLINE
| ID: mdl-26916536
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.
Full text:
1
Database:
MEDLINE
Main subject:
Oligopeptides
/
Protein Denaturation
/
Protein Structure, Secondary
/
Cold Temperature
Language:
En
Year:
2016
Type:
Article