True Solid-State Electrical Conduction of Proteins shows them to be Efficient Transport Media
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arXiv
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| Autori principali: | , , , , , , |
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| Natura: | Preprint |
| Pubblicazione: |
2025
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| _version_ | 1866913808032727040 |
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| author | Bera, Sudipta Vilan, Ayelet Das, Sourav Pecht, Israel Ehre, David Sheves, Mordechai Cahen, David |
| author_facet | Bera, Sudipta Vilan, Ayelet Das, Sourav Pecht, Israel Ehre, David Sheves, Mordechai Cahen, David |
| contents | While solid-state protein junctions have shown efficient electron transport over lengths that surpass those of conventional organic semiconducting systems, interfacial or contact effects may obscure the intrinsic protein charge transport properties. Therefore, contact resistance (RC) effects need to be quantified and then minimized, which poses a problem if 4-probe geometries cannot be used. Here we show how RC can be extracted quantitatively from the measured junction resistance (RP) by using the extrapolated zero-length resistance (RZLR) and short-circuit resistance (RS). We used AC (impedance spectroscopy) and DC measurements to examine charge transport in junctions of human serum albumin (HSA) and bacteriorhodopsin (bR) films with varying thicknesses. Three contact configurations, Si-Au, Au-EGaIn, and, in a micropore device (MpD), Au-Pd, were compared. While Si-Au and Au-EGaIn junctions exhibit substantial RC that we ascribe to interfacial oxides and electrostatic protein-electrode interactions, MpD effectively eliminates RC, enabling measuring the intrinsic electron transport across HSA and bR films. The exponential length dependence of RP shows a transport decay constant (beta) that varies with interfacial conditions, underscoring the role of contact engineering. By minimizing RC, exceptionally low beta values (0.7 to 1.1 per nm) are found, proving that, indeed, proteins can have outstanding charge transport efficiencies. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2504_18552 |
| institution | arXiv |
| publishDate | 2025 |
| record_format | arxiv |
| spellingShingle | True Solid-State Electrical Conduction of Proteins shows them to be Efficient Transport Media Bera, Sudipta Vilan, Ayelet Das, Sourav Pecht, Israel Ehre, David Sheves, Mordechai Cahen, David Biological Physics Disordered Systems and Neural Networks Mesoscale and Nanoscale Physics Soft Condensed Matter Applied Physics While solid-state protein junctions have shown efficient electron transport over lengths that surpass those of conventional organic semiconducting systems, interfacial or contact effects may obscure the intrinsic protein charge transport properties. Therefore, contact resistance (RC) effects need to be quantified and then minimized, which poses a problem if 4-probe geometries cannot be used. Here we show how RC can be extracted quantitatively from the measured junction resistance (RP) by using the extrapolated zero-length resistance (RZLR) and short-circuit resistance (RS). We used AC (impedance spectroscopy) and DC measurements to examine charge transport in junctions of human serum albumin (HSA) and bacteriorhodopsin (bR) films with varying thicknesses. Three contact configurations, Si-Au, Au-EGaIn, and, in a micropore device (MpD), Au-Pd, were compared. While Si-Au and Au-EGaIn junctions exhibit substantial RC that we ascribe to interfacial oxides and electrostatic protein-electrode interactions, MpD effectively eliminates RC, enabling measuring the intrinsic electron transport across HSA and bR films. The exponential length dependence of RP shows a transport decay constant (beta) that varies with interfacial conditions, underscoring the role of contact engineering. By minimizing RC, exceptionally low beta values (0.7 to 1.1 per nm) are found, proving that, indeed, proteins can have outstanding charge transport efficiencies. |
| title | True Solid-State Electrical Conduction of Proteins shows them to be Efficient Transport Media |
| topic | Biological Physics Disordered Systems and Neural Networks Mesoscale and Nanoscale Physics Soft Condensed Matter Applied Physics |
| url | https://arxiv.org/abs/2504.18552 |