Chiral inorganic nanomaterials have revealed opportunities in various fields owing to their strong light–matter interactions. In particular, chiral metal oxide nanomaterials that can control light and biochemical reactions have been highlighted due to their catalytic activity and biocompatibility. In this study, we present the synthesis of chiral cobalt oxide nanoparticles with a g-factor of 0.01 in the UV–visible region using l- and d-Tyr-Tyr-Cys ligands. The conformation of the Tyr-Tyr-Cys peptide on the nanoparticle surfaces was identified by 2D NMR spectroscopy analysis. In addition, the sequence effect of Tyr-Tyr-Cys developing chiral nanoparticles was analyzed. The revealed peptide structure, along with the experimental results, demonstrate the important role of the thiol group and carboxyl group of the Tyr-Tyr-Cys ligand in chirality evolution. Importantly, due to the magnetic properties of chiral cobalt oxide nanoparticles and their strong absorption in the UV region, the circular dichroism (CD) responses can be dramatically modulated under an external magnetic field.

Squamous cell carcinoma antigen recognized by T-cells 3 (SART3) is an essential recycling factor in pre-mRNA splicing, which is required for association of U4/U6 small nuclear ribonucleoprotein (snRNP). SART3 contains two RNA recognition motifs (RRMs), and they are responsible for the tertiary interaction with U6 small nuclear RNA. Despite the importance of structural studies for understanding complicate U4/U6 snRNP recycling mechanism, only a few of them have been performed for SART3. Here, the structure of SART3 RRM2 was characterized by heteronuclear multi-dimensional nuclear magnetic resonance experiments. Nearly complete 1 H, 15 N, and 13 C chemical shifts of the backbone residues of RRM2 were assigned. In addition, the secondary structure of RRM2 were predicted by the chemical shift index and TALOS+ analyses, and the results showed that RRM2 forms a "β 1 -α 1 -β 2 -β 3 -α 2 -β 4 -β 5 " structure, where β 4 is not common in the canonical RRM domain structures. Our results will provide structural basis for investigation of SART3-mediated U4/U6 snRNP complex formation. Figure 3.Strip plots from the CBCA(CO)NH and HNCACB spectra used for sequential assignment of SART3 RRM2. Sequential C α and C β connectivity for the residues L803-L808 is shown with solid lines. ArticleStructural Characterization of the RRM2 Domain of SART3