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Plastic has significant negative consequences for the environment and human health, demanding greener alternatives. Lignocellulose is a sustainable biomass material, and its paper has been considered as a potential material to replace plastics. Micro-nano lignocellulose, derived from natural plants, possesses a small size and abundant hydrogen bonding capacity. However, there is no clear explanation for the interactions between lignin and micro-nano cellulose, and little understanding of how the interaction can affect the papers' structure and optical properties. Electrostatic potential calculation is a reliable tool to explain non-covalent interactions, and can explore the binding between lignin and micro-nano cellulose. In this paper, kenaf – a non-wood fiber raw material – was employed to prepare micro-nano lignocellulose. The resulting slurry facilitated the production of transparent paper via a simple casting method. The prepared transparent micro-nano paper exhibited high transparency (~90 %), UVA resistance (~80 %), and hydrophobicity (~114°). More importantly, the electrostatic potential calculation demonstrates the inherent relationship between structure and performance, providing practical knowledge for constructing film materials. [Display omitted] [ABSTRACT FROM AUTHOR]

Abstract: In Bacillus subtilis, CodW peptidase and CodX ATPase function together as a distinctive ATP-dependent protease called CodWX, which participates in protein degradation and regulates cell division. The molecular structure of CodX and the assembly structure of CodW–CodX have not yet been resolved. Here we present the first three-dimensional structure of CodX N-terminal (N) and C-terminal (C) domain including possible structure of intermediate (I) domain based on the crystal structure of homologous Escherichia coli HslU ATPase. Moreover, the biologically relevant CodWX (W6W6X6) octadecamer complex structure was constructed using the recently identified CodW–HslU hybrid crystal structure. Molecular dynamics (MD) simulation shows a reasonably stable structure of modeled CodWX and explicit behavior of key segments in CodX N and C domain: nucleotide binding residues, GYVG pore motif and CodW–CodX interface. Predicted structure of the possible I domain is flexible in nature with highly coiled hydrophobic region (M153–M206) that could favor substrate binding and entry. Electrostatic surface potential observation unveiled charge complementarity based CodW–CodX interaction pattern could be a possible native interaction pattern in the interface of CodWX. CodX GYVG pore motif structural features, flexible nature of glycine (G92 and G95) residues and aromatic ring conformation preserved Y93 indicated that it may follow the similar mode during the proteolysis mechanism as in the HslU closed state. This molecular modeling study uncovers the significance of CodX N and C domain in CodWX complex and provides possible explanations which would be helpful to understand the CodWX-dependent proteolysis mechanism of B. subtilis. [Copyright &y& Elsevier]