Simultaneous achievement of good electrochemical and mechanical properties is crucial for practical applications of solid ion conductors. Conventional polymer conductors suffer from low conductivity, low transference number, and deteriorated mechanical properties with the enhancement of conductivity, resulting from the coupling between ion transport and polymer movement. Here we present a successful fabrication and fundamental understanding of a high performance soy protein-based solid conductor. The conductor shows ionic conductivity of ∼10 S/cm, transference number of 0.94, and modulus of 1 GPa at room temperature, and still remains flexible and easily processable. Molecular simulations indicate that this is due to appropriate manipulation of the protein structures for effective exploitation of protein functional groups. A decoupled transport mechanism, which is able to explain all results, is proposed. The new insights can be utilized to provide guidelines for design, optimization, and fabrication of high performance biosolid conductors.

The multidrug resistance (MDR) system actively pumps the antibiotics out of cells causing serious health problems. During the pumping, AcrB (one of the key MDR components), undergoes a series of large-scale and proton-motive conformational changes. Capturing the conformational changes through all-atom simulations is challenging. Here, we implement a hybrid coarse-grained force field to investigate the conformational changes of AcrB in porter domain under different protonation states of Asp407/Asp408 in trans-membrane domain. Our results show that protonation of Asp408 in monomer III (extrusion) stabilizes the asymmetric structure of AcrB; deprotonation of Asp408 induces clear opening of the entrance and closing of the exit leading to the transition from extrusion to access state. The structural changes in porter domain of AcrB are strongly coupled with the proton translocation stoichiometry in trans-membrane domain. Moreover, our simulations support the postulation that the AcrB should adopt the symmetric resting state in a substrate-free situation.

The multidrug resistance (MDR) system effectively expels antibiotics out of bacteria causing serious issues during bacterial infection. In addition to drug, indole, a common metabolic waste of bacteria, is expelled by MDR system of gram‐negative bacteria for their survival. Experimental results suggest that AcrB, one of the key components of MDR system, undergoes large scale conformation changes during the pumping due to proton‐motive process. However, due to extremely short time scale, it is difficult to observe (experimentally) those changes in the AcrB, which might facilitate the pumping process. Molecular simulations can shed light to understand the conformational changes for transport of indole in AcrB. Examination of conformational changes using all‐atom simulation is, however, impractical. Here, we develop a hybrid coarse‐grained force field to study the conformational changes of AcrB in presence of indole in the porter domain of monomer II. Using the coarse‐grained force field, we investigated the conformational changes of AcrB for a number of model systems considering the effect of protonation in aspartic acid (Asp) residues Asp407 and Asp408 in the transmembrane domain of monomer II. Our results show that in the presence of indole, protonation of Asp408 or Asp407 residue causes conformational changes from binding state to extrusion state in monomer II, while remaining two monomers (I and III) approach access state in AcrB protein. We also observed that all three AcrB monomers prefer to go back to access state in the absence of indole. Steered molecular dynamics simulations were performed to demonstrate the feasibility of indole transport mechanism for protonated systems. Identification of indole transport pathway through AcrB can be very helpful in understanding the drug efflux mechanism used by the MDR bacteria.

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