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Developing hydrolytic nanozymes remains challenging. Here the authors present a rational methodology to design hydrolytic nanozyme by developing a data-informed strategy to screen and identify potential scaffold and active sites of hydrolase-like nanozyme.

Electrocatalytic carbon dioxide (CO2) reduction is considered as an economical and environmentally friendly approach to neutralizing and recycling greenhouse gas CO2. However, the design of preeminent and robust electrocatalysts for CO2 electroreduction is still challenging. Herein, we report the in-situ growth of dense CuOx nanowire forest on 3D porous Cu foam (CuOx-NWF@Cu-F), which can be directly applied as a freestanding and binder-free working electrode for highly effective electrocatalytic CO2 reduction. By adjusting the surface morphology and chemical composition of CuOx nanowires via surface reconstruction, large electrochemically active surface area and abundant Cu(+1) sites were generated, leading to remarkable activity for CO2 electroreduction. The as-prepared hierarchical conductive electrode exhibited an enhanced Faradaic efficiency of 15.0% for ethanol formation (FEC2H5OH) and a total Faradaic efficiency of 69.4% for all carbonaceous compounds (FEC-total) at a mild applied potential of –0.45 V vs. RHE in 0.1 M KHCO3 electrolyte. It achieved a 4-fold increase in FEC-total than that of Cu nanowire forest supported on 3D porous Cu foam (Cu-NWF@Cu-F) obtained by in-situ reduction of the CuOx-NWF@Cu-F via annealing at H2 atmosphere, and thereby effectively suppressed the hydrogen evolution side-reaction.

We investigated the effects of solvents on the intrinsic propensity of peptide backbone conformations based on molecular dynamics simulations. The results show that compared with pure water, aqueous urea decreases the helix propensity. In comparison, methanol decreases the polyproline II (PPII) propensity. Such a solvent dependence of the intrinsic propensity of the backbone conformation is correlated with the solvent dependence of the hydration of the backbone groups and the formation probability of the local intrapeptide hydrogen bonds. Aqueous urea which has low ability to stabilize the local intrapeptide hydrogen bonds disfavors the helical conformation. Whereas, methanol which has low ability to hydrate the backbone groups disfavors the polyproline II conformation. In addition, the solvent effects can be further modulated by the side chains of the peptides. The solvent effects of the intrinsic propensity of peptide backbone conformations observed in this work suggest that changing the intrinsic propensity of the protein backbone conformations can partly contribute to the solvent-induced protein structure and dynamics variations. These results will be useful in understanding the solvent dependence of the conformational distributions of the unfolded proteins or peptides (or intrinsically disordered proteins) in which the global tertiary interactions are less important than that in the well-folded proteins. [ABSTRACT FROM AUTHOR]