Multiferroic hydrogenated graphene bilayer.

We investigated the multiferroic properties of a hydrogenated graphene bilayer using first-principles calculations. The proposed material is composed of one fully hydrogenated and one semi-hydrogenated graphene monolayer. Inside the van der Waals gap, hydrogen atoms are only adsorbed on either the top or the bottom layer of graphene, thus breaking the centrosymmetry. The calculated electric polarization is 0.137 × 10-10 C m-1, with the transition barrier of switching the polarization being 393 meV per formula unit. We showed that ferroelectricity can be preserved down to atomic thickness. We also studied the domain wall energy and its migration for various domain wall densities, and our results indicate a robust polarization configuration against room temperature thermal fluctuation. As graphene is known to be able to sustain large strain, we further explored ferroelectricity tuning via strain, and found that the polarization can be effectively tuned up to 20% without perturbing the polarization switching barrier. Our results suggest a realizable multiferroic two-dimensional material using the most used two-dimensional material, graphene.

The cysteine-free single mutant C32S of APEX2 is a highly expressed and active fusion tag for proximity labeling applications.

APEX2, an engineered ascorbate peroxidase for high activity, is a powerful tool for proximity labeling applications. Owing to its lack of disulfides and the calcium-independent activity, APEX2 can be applied intracellularly for targeted electron microscopy imaging or interactome mapping when fusing to a protein of interest. However, APEX2 fusion is often deleterious to the protein expression, which seriously hampers its wide utility. This problem is especially compelling when APEX2 is fused to structurally delicate proteins, such as multi-pass membrane proteins. In this study, we found that a cysteine-free single mutant C32S of APEX2 dramatically improved the expression of fusion proteins in mammalian cells without compromising the enzyme activity. We fused APEX2 and APEX2C32S to four multi-transmembrane solute carriers (SLCs), SLC1A5, SLC6A5, SLC6A14, and SLC7A1, and compared their expressions in stable HEK293T cell lines. Except the SLC6A5 fusions expressing at decent levels for both APEX2 (70%) and APEX2C32S (73%), other three SLC proteins showed significantly better expression when fusing to APEX2C32S (69 ± 13%) than APEX2 (29 ± 15%). Immunofluorescence and western blot experiments showed correct plasma membrane localization and strong proximity labeling efficiency in all four SLC-APEX2C32S cells. Enzyme kinetic experiments revealed that APEX2 and APEX2C32S have comparable activities in terms of oxidizing guaiacol. Overall, we believe APEX2C32S is a superior fusion tag to APEX2 for proximity labeling applications, especially when mismatched disulfide bonding or poor expression is a concern.