Temperature and force dependence of nanoscale electron transport via the Cu protein Azurin
Wenjie Li, Lior Sepunaru, Nadav Amdursky, Sidney R. Cohen, Israel, Pecht, Mordechai Sheves, David Cahen

TL;DR
This study investigates how temperature and applied force influence electron transport in Azurin proteins at the nanoscale, revealing that mechanical stress can alter the transport mechanism and emphasizing the importance of controlling force during measurements.
Contribution
It demonstrates that the electron transport mechanism in Azurin proteins depends on applied force and temperature, highlighting the role of mechanical stress in nanoscale electron transport.
Findings
ETp mechanism shifts from temperature-independent to thermally activated with increased force
Holo-Az and apo-Az show different responses to force and temperature
Stress control is crucial for accurate ETp measurements in flexible systems
Abstract
The mechanisms of solid-state electron transport (ETp) via a monolayer of immobilized Azurin (Az) was examined by conducting probe atomic force microscopy (CP-AFM), both as function of temperature (248 - 373K) and of applied tip force (6-12 nN). By varying both temperature and force in CP-AFM, we find that the ETp mechanism can alter with a change in the force applied via the tip to the proteins. As the applied force increases, ETp via Az changes from temperature-independent to thermally activated at high temperatures. This is in contrast to the Cu-depleted form of Az (apo-Az), where increasing the applied force causes only small quantitative effects, that fit with a decrease in electrode spacing. At low force ETp via holo-Az is temperature-independent and thermally activated via apo-Az. This observation agrees with macroscopic-scale measurements, thus confirming that the difference in…
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