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Protein Conformation Governs Spin-Selective Electron Transmission
Naupada Preeyanka1, Tapan Kumar Das1, Ron Naaman1
1Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot 7610001, Israel.
The chiral induced spin selectivity (CISS) effect in proteins is significantly reduced upon denaturation. This highlights the crucial role of protein secondary structure in maintaining spin polarization for biological systems.
Area of Science:
- Biophysics
- Materials Science
- Biochemistry
Background:
- Chiral induced spin selectivity (CISS) describes spin-dependent electron transport in chiral molecules.
- Proteins possess chirality in their primary (amino acids) and secondary (helical structures) conformations.
- Understanding the contribution of each chirality type to CISS in biological systems is crucial.
Purpose of the Study:
- To investigate the impact of protein denaturation on spin polarization.
- To differentiate the roles of primary and secondary structures in chiral spin selectivity.
- To use d-glucose oxidase (GOx) as a model system to study these effects.
Main Methods:
- Comparison of spin selective behavior of GOx in native and thermally denatured states.
- Utilizing Hall-effect and magnetoresistance (MR) measurements.
- Thermal denaturation at 65 °C and 95 °C.
Main Results:
- Native GOx exhibits strong spin polarization, linked to its helical structure and FAD cofactor.
- Thermal denaturation significantly reduces spin polarization, evidenced by decreased Hall voltage slope and MR values.
- Loss of spin polarization correlates with the disruption of the protein's secondary structure.
Conclusions:
- Protein secondary structure is essential for maintaining chiral potential landscapes and high spin polarization.
- Denaturation disrupts secondary structure, leading to a loss of spin selectivity.
- Spin-related structural properties remain even when the protein is integrated into a device.
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